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Conserved domains on  [gi|446800108|ref|WP_000877364|]
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MULTISPECIES: intercellular adhesin biosynthesis polysaccharide N-deacetylase [Staphylococcus]

Protein Classification

5-oxoprolinase subunit PxpA; glycoside hydrolase family 38 protein( domain architecture ID 10024213)

5-oxoprolinase subunit PxpA catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate| glycosyl hydrolase family 38 (GH38) protein such as human core-specific lysosomal alpha 1,6-mannosidase (Epman, Man2B2) which can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharide

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PIA_icaB TIGR03933
intercellular adhesin biosynthesis polysaccharide N-deacetylase; A common motif in bacterial ...
43-287 6.53e-152

intercellular adhesin biosynthesis polysaccharide N-deacetylase; A common motif in bacterial biosynthesis of polysaccharide for export is modification that follows polymerization. This model describes a subfamily of polysaccharide N-deacetylases that acts on poly-beta-1,6-N-acetyl-D-glyscosamine as produced by Staphylococcus epidermidis and S. aureus. The end product in these species is designated polysaccharide intercellular adhesin (PIA), and this gene designated icaB (intercellular adhesion protein B). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Cellular processes, Pathogenesis]


:

Pssm-ID: 188448 [Multi-domain]  Cd Length: 245  Bit Score: 424.62  E-value: 6.53e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108   43 NSALALNYHRVRKANFLNNFIYFFSSSKEIKNYSVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGKFPKRSVWINFDD 122
Cdd:TIGR03933   1 NSALALNYHRVRKDDPLNNFISLLSSSKEIKNYSVSDSEFESQIKWLKAHDAKFLTLKEFIKYKEKGKFPKRSVWINFDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  123 MDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLDMISKKELKEMYKTGLWEFETHTHDLHNLSKNNKSKLMKSSEA 202
Cdd:TIGR03933  81 MDQTIYDNAFPILKKYKIPATGFVITGHIGDENFHNLNLIDLKQLKEMYATGLWDFESHTHDLHNLKKSNKSKFLHSSKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  203 TIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILISDDAFEHLIKR 282
Cdd:TIGR03933 161 GAKKDIDKSEKYLNKNFNKNQTSIAYPYGLINDDKIKVLKKAGIRYGFTLEEKAVTPDDNNYRIPRILVSNDAFEKLIKK 240

                  ....*
gi 446800108  283 WDGFH 287
Cdd:TIGR03933 241 WDGFN 245
 
Name Accession Description Interval E-value
PIA_icaB TIGR03933
intercellular adhesin biosynthesis polysaccharide N-deacetylase; A common motif in bacterial ...
43-287 6.53e-152

intercellular adhesin biosynthesis polysaccharide N-deacetylase; A common motif in bacterial biosynthesis of polysaccharide for export is modification that follows polymerization. This model describes a subfamily of polysaccharide N-deacetylases that acts on poly-beta-1,6-N-acetyl-D-glyscosamine as produced by Staphylococcus epidermidis and S. aureus. The end product in these species is designated polysaccharide intercellular adhesin (PIA), and this gene designated icaB (intercellular adhesion protein B). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Cellular processes, Pathogenesis]


Pssm-ID: 188448 [Multi-domain]  Cd Length: 245  Bit Score: 424.62  E-value: 6.53e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108   43 NSALALNYHRVRKANFLNNFIYFFSSSKEIKNYSVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGKFPKRSVWINFDD 122
Cdd:TIGR03933   1 NSALALNYHRVRKDDPLNNFISLLSSSKEIKNYSVSDSEFESQIKWLKAHDAKFLTLKEFIKYKEKGKFPKRSVWINFDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  123 MDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLDMISKKELKEMYKTGLWEFETHTHDLHNLSKNNKSKLMKSSEA 202
Cdd:TIGR03933  81 MDQTIYDNAFPILKKYKIPATGFVITGHIGDENFHNLNLIDLKQLKEMYATGLWDFESHTHDLHNLKKSNKSKFLHSSKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  203 TIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILISDDAFEHLIKR 282
Cdd:TIGR03933 161 GAKKDIDKSEKYLNKNFNKNQTSIAYPYGLINDDKIKVLKKAGIRYGFTLEEKAVTPDDNNYRIPRILVSNDAFEKLIKK 240

                  ....*
gi 446800108  283 WDGFH 287
Cdd:TIGR03933 241 WDGFN 245
CE4_IcaB_5s cd10965
Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion ...
112-284 1.49e-68

Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion protein IcaB and similar proteins; The family is represented by the surface-attached protein intercellular adhesion protein IcaB (Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase, EC 3.5.1.-), encoded by Staphylococcus epidermidis icaB gene from the icaABC gene cluster that is involved in the synthesis of polysaccharide intercellular adhesin (PIA), which is located mainly on the cell surface. IcaB is a secreted, cell wall-associated protein that plays a crucial role in exopolysaccharide modification in bacterial biofilm formation. It catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. IcaB shows high homology to the N-terminal NodB homology domain of Escherichia coli PgaB. At this point, they are classified in the same family.


Pssm-ID: 200587 [Multi-domain]  Cd Length: 172  Bit Score: 210.32  E-value: 1.49e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 112 PKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEENFhNLDMISKKELKEMYKTGLWEFETHTHDLHNLSKN 191
Cdd:cd10965    1 PGKYVVITFDDVDQTVYDNAFPILKKLKIPFTQFVITGQVGSTNF-GLNLATWSQIKEMVASGLVTFGLHTNDLHYLVKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 192 NKSKLMKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILI 271
Cdd:cd10965   80 KKKLFTPASYSRFAEDYAKSQKCLKEKLGKKTRYFAYPYGEGNKDTQKILKKQGIQYGFTLRDKVVTNDSDNYRIPRILV 159
                        170
                 ....*....|...
gi 446800108 272 SDDAFEHLIKRWD 284
Cdd:cd10965  160 TNDSFWKLIKKWI 172
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
108-249 2.72e-34

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 120.80  E-value: 2.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  108 KGKFPKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEEnfhnldmisKKELKEMYKTGlWEFETHTHDLHN 187
Cdd:pfam01522   1 KGPTPKKVVALTFDDGPSENTPAILDVLKKYGVKATFFVIGGNVERY---------PDLVKRMVEAG-HEIGNHTWSHPN 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446800108  188 LSknnksklmKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYG 249
Cdd:pfam01522  71 LT--------GLSPEEIRKEIERAQDALEKATGKRPRLFRPPYGSYNDTVLEVAKKLGYTAV 124
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
96-283 3.49e-27

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440490 [Multi-domain]  Cd Length: 195  Bit Score: 104.74  E-value: 3.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  96 FLTLKEFLYYKKKGKFPKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEenfhnldmiSKKELKEMYKTGl 175
Cdd:COG0726    2 VLSLDELLPALRWGPLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVER---------HPELVREIAAAG- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 176 WEFETHTHDLHNLSknnksklmKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGF----- 250
Cdd:COG0726   72 HEIGNHTYTHPDLT--------KLSEEEERAEIARAKEALEELTGKRPRGFRPPYGRYSPETLDLLAELGYRYILwdsvd 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446800108 251 -----SLEEKAVTPNSNDYYIPRILISD--DAFEHLIKRW 283
Cdd:COG0726  144 sddwpYPSADAIVDRVLKYLKPGSIRPGtvEALPRLLDYL 183
hmsF PRK14581
outer membrane N-deacetylase; Provisional
34-274 1.62e-16

outer membrane N-deacetylase; Provisional


Pssm-ID: 184753 [Multi-domain]  Cd Length: 672  Bit Score: 79.64  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  34 PPKKLKYKENSALALNYHRVRkanflnnfiyffSSSKEIKNYSVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGK-FP 112
Cdd:PRK14581  38 PQSERPWQKNTFVVIAYHDVE------------DDSADQRYLSVRSSALNEQFVWLRDNGYHVVSVDQILAARNGGPtLP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 113 KRSVWINFDDMDETIYENAYPILKKYKIPA----TGFIITGHVGEE-NFHNLD-----MISKKELKEMYKTGLWEFETHT 182
Cdd:PRK14581 106 DKAVLLTFDDGYSSFYRRVYPLLKAYKWSAvlapVGTWIDTATDKKvDFGGLStdrdrFATWKQITEMSKSGLVEIGAHT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 183 HDLH----------------NLSKNNKSKLMKSSEA---TIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKK 243
Cdd:PRK14581 186 YASHygvianpqgntepaaaNLQYDPKTKQYETVEAfkqRMEKDVALITQRIVQATGKQPRVWVWPYGAPNGTVLNILRQ 265
                        250       260       270
                 ....*....|....*....|....*....|..
gi 446800108 244 AGLKYGFSLEEKAVtpNSNDYY-IPRILISDD 274
Cdd:PRK14581 266 HGYQLAMTLDPGVA--NINDLMnIPRILISNN 295
 
Name Accession Description Interval E-value
PIA_icaB TIGR03933
intercellular adhesin biosynthesis polysaccharide N-deacetylase; A common motif in bacterial ...
43-287 6.53e-152

intercellular adhesin biosynthesis polysaccharide N-deacetylase; A common motif in bacterial biosynthesis of polysaccharide for export is modification that follows polymerization. This model describes a subfamily of polysaccharide N-deacetylases that acts on poly-beta-1,6-N-acetyl-D-glyscosamine as produced by Staphylococcus epidermidis and S. aureus. The end product in these species is designated polysaccharide intercellular adhesin (PIA), and this gene designated icaB (intercellular adhesion protein B). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Cellular processes, Pathogenesis]


Pssm-ID: 188448 [Multi-domain]  Cd Length: 245  Bit Score: 424.62  E-value: 6.53e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108   43 NSALALNYHRVRKANFLNNFIYFFSSSKEIKNYSVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGKFPKRSVWINFDD 122
Cdd:TIGR03933   1 NSALALNYHRVRKDDPLNNFISLLSSSKEIKNYSVSDSEFESQIKWLKAHDAKFLTLKEFIKYKEKGKFPKRSVWINFDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  123 MDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLDMISKKELKEMYKTGLWEFETHTHDLHNLSKNNKSKLMKSSEA 202
Cdd:TIGR03933  81 MDQTIYDNAFPILKKYKIPATGFVITGHIGDENFHNLNLIDLKQLKEMYATGLWDFESHTHDLHNLKKSNKSKFLHSSKA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  203 TIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILISDDAFEHLIKR 282
Cdd:TIGR03933 161 GAKKDIDKSEKYLNKNFNKNQTSIAYPYGLINDDKIKVLKKAGIRYGFTLEEKAVTPDDNNYRIPRILVSNDAFEKLIKK 240

                  ....*
gi 446800108  283 WDGFH 287
Cdd:TIGR03933 241 WDGFN 245
CE4_IcaB_5s cd10965
Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion ...
112-284 1.49e-68

Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion protein IcaB and similar proteins; The family is represented by the surface-attached protein intercellular adhesion protein IcaB (Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase, EC 3.5.1.-), encoded by Staphylococcus epidermidis icaB gene from the icaABC gene cluster that is involved in the synthesis of polysaccharide intercellular adhesin (PIA), which is located mainly on the cell surface. IcaB is a secreted, cell wall-associated protein that plays a crucial role in exopolysaccharide modification in bacterial biofilm formation. It catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. IcaB shows high homology to the N-terminal NodB homology domain of Escherichia coli PgaB. At this point, they are classified in the same family.


Pssm-ID: 200587 [Multi-domain]  Cd Length: 172  Bit Score: 210.32  E-value: 1.49e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 112 PKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEENFhNLDMISKKELKEMYKTGLWEFETHTHDLHNLSKN 191
Cdd:cd10965    1 PGKYVVITFDDVDQTVYDNAFPILKKLKIPFTQFVITGQVGSTNF-GLNLATWSQIKEMVASGLVTFGLHTNDLHYLVKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 192 NKSKLMKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILI 271
Cdd:cd10965   80 KKKLFTPASYSRFAEDYAKSQKCLKEKLGKKTRYFAYPYGEGNKDTQKILKKQGIQYGFTLRDKVVTNDSDNYRIPRILV 159
                        170
                 ....*....|...
gi 446800108 272 SDDAFEHLIKRWD 284
Cdd:cd10965  160 TNDSFWKLIKKWI 172
CE4_NodB_like_5s_6s cd10918
Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a ...
115-274 3.70e-37

Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a deformed (beta/alpha)8 barrel fold with 5- or 6-strands; This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, hemin storage system HmsF protein in gram-negative species, intercellular adhesion proteins IcaB, and many uncharacterized prokaryotic polysaccharide deacetylases. It also includes a putative polysaccharide deacetylase YxkH encoded by the Bacillus subtilis yxkH gene, which is one of six polysaccharide deacetylase gene homologs present in the Bacillus subtilis genome. Sequence comparison shows all family members contain a conserved domain similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, which consists of a deformed (beta/alpha)8 barrel fold with 6 or 7 strands. However, in this family, most proteins have 5 strands and some have 6 strands. Moreover, long insertions are found in many family members, whose function remains unknown.


Pssm-ID: 213023 [Multi-domain]  Cd Length: 157  Bit Score: 129.25  E-value: 3.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 115 SVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLD------MISKKELKEMYKTGlWEFETHTHDlHnl 188
Cdd:cd10918    1 PVVLTFDDGYRDNYTYALPILKKYGLPATFFVITGYIGGGNPWWAPapprppYLTWDQLRELAASG-VEIGSHTHT-H-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 189 sknnkSKLMKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPR 268
Cdd:cd10918   77 -----PDLTTLSDEELRRELAESKERLEEELGKPVRSFAYPYGRYNPRVIAALKEAGYKAAFTTDPGLNSPGDDPYALPR 151

                 ....*.
gi 446800108 269 ILISDD 274
Cdd:cd10918  152 INVSGD 157
CE4_yadE_5s cd10966
Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and ...
112-275 3.46e-36

Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and similar proteins; This family contains an uncharacterized protein yadE from Escherichia coli and its bacterial homologs. Although its molecular function remains unknown, yadE shows high sequence similarity with the catalytic NodB homology domain of outer membrane lipoprotein PgaB and the surface-attached protein intercellular adhesion protein IcaB. Both PgaB and IcaB are essential in bacterial biofilm formation.


Pssm-ID: 213024 [Multi-domain]  Cd Length: 164  Bit Score: 127.01  E-value: 3.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 112 PKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGE--ENFHNLDMISKKELKEMykTGLWEFETHTHDLHNLS 189
Cdd:cd10966    1 PEKSVVITFDDGYKSNYEYAYPILKKYGFKATIFVIGSRIGEkpQDPKILQYLSIEELKEM--RDVFEFQSHTYNMHRGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 190 KNNKSKLMKSSEATIIKDLNKSEKYLtknfkKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRI 269
Cdd:cd10966   79 GTGGHGLLALSEEEILADLKKSEEIL-----GSSKAFAYPYGDYNDNAIEALKEAGVKLAFTTNEGKVTPGDDPYELPRV 153

                 ....*.
gi 446800108 270 LISDDA 275
Cdd:cd10966  154 RITGGT 159
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
108-249 2.72e-34

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 120.80  E-value: 2.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  108 KGKFPKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEEnfhnldmisKKELKEMYKTGlWEFETHTHDLHN 187
Cdd:pfam01522   1 KGPTPKKVVALTFDDGPSENTPAILDVLKKYGVKATFFVIGGNVERY---------PDLVKRMVEAG-HEIGNHTWSHPN 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446800108  188 LSknnksklmKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYG 249
Cdd:pfam01522  71 LT--------GLSPEEIRKEIERAQDALEKATGKRPRLFRPPYGSYNDTVLEVAKKLGYTAV 124
CE4_Ecf1_like_5s cd10969
Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli ...
81-282 9.91e-34

Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli and similar proteins; This family contains a hypothetical protein Ecf1 from Escherichia coli and its prokaryotic homologs. Although their biochemical properties remain to be determined, members in this family contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213026 [Multi-domain]  Cd Length: 218  Bit Score: 122.40  E-value: 9.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  81 QFESQIKWLKSHDAKFLTLKEFLYYKKKGK-FPKRSVWINFDD--MDETIYenAYPILKKYKIPATGFIITGHVGEENFH 157
Cdd:cd10969    3 TFEEQLKYLKKNGYRTLSLEELLAFLKGGKpLPKKSVLITFDDgyLDNYVY--AYPILKKYGLKATIFVVTGFIDEASGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 158 ------------------------NLDMISKKELKEMYKTGLWEFETHTHDlHNLsknnksklmksseatIIKDLNKSEK 213
Cdd:cd10969   81 rptlfdywsgdmpeankifflkgrDEVFLSWEELREMEDSGVFDIQSHSHS-HTR---------------VEYELEESKR 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446800108 214 YLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILISDDAFEHLIKR 282
Cdd:cd10969  145 LLEENLGKKVDHFCWPWGHYSPESLRIAKELGFKFFFTTKKGVNVPGEDPDRIKRITVKKDGGFWLKKR 213
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
96-283 3.49e-27

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440490 [Multi-domain]  Cd Length: 195  Bit Score: 104.74  E-value: 3.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  96 FLTLKEFLYYKKKGKFPKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEenfhnldmiSKKELKEMYKTGl 175
Cdd:COG0726    2 VLSLDELLPALRWGPLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVER---------HPELVREIAAAG- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 176 WEFETHTHDLHNLSknnksklmKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGF----- 250
Cdd:COG0726   72 HEIGNHTYTHPDLT--------KLSEEEERAEIARAKEALEELTGKRPRGFRPPYGRYSPETLDLLAELGYRYILwdsvd 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446800108 251 -----SLEEKAVTPNSNDYYIPRILISD--DAFEHLIKRW 283
Cdd:COG0726  144 sddwpYPSADAIVDRVLKYLKPGSIRPGtvEALPRLLDYL 183
CE4_PgaB_5s cd10964
N-terminal putative catalytic polysaccharide deacetylase domain of bacterial poly-beta-1, ...
112-274 8.81e-25

N-terminal putative catalytic polysaccharide deacetylase domain of bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, and similar proteins; This family is represented by an outer membrane lipoprotein, poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (PgaB, EC 3.5.1.-), encoded by Escherichia coli pgaB gene from the pgaABCD (formerly ycdSRQP) operon, which affects biofilm development by promoting abiotic surface binding and intercellular adhesion. PgaB catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide that stabilizes biofilms of E. coli and other bacteria. PgaB contains an N-terminal NodB homology domain with a 5-stranded beta/alpha barrel, and a C-terminal carbohydrate binding domain required for PGA N-deacetylation, which may be involved in binding to unmodified poly-beta-1,6-GlcNAc and assisting catalysis by the deacetylase domain. This family also includes several orthologs of PgaB, such as the hemin storage system HmsF protein, encoded by Yersinia pestis hmsF gene from the hmsHFRS operon, which is essential for Y. pestis biofilm formation. Like PgaB, HmsF is an outer membrane protein with an N-terminal NodB homology domain, which is likely involved in the modification of the exopolysaccharide (EPS) component of the biofilm. HmsF also has a conserved but uncharacterized C-terminal domain that is present in other HmsF-like proteins in Gram-negative bacteria. This alignment model corresponds to the N-terminal NodB homology domain.


Pssm-ID: 200586 [Multi-domain]  Cd Length: 193  Bit Score: 98.18  E-value: 8.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 112 PKRSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHV----------GEENFHNLDMISKKELKEMYKTGLWEFETH 181
Cdd:cd10964    2 PAKAVLLTFDDGYQSFYTRVYPLLKAYKYPAVLALVGSWLetpagkkvdyGGEQLPRDRFLSWEQIREMQASGLVEIASH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 182 THDLHNLSKNN---------------KSKLMKSSEAT----IIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIK 242
Cdd:cd10964   82 SHDLHHGIPANpqgnllpaattrqydPKTGRYETDAEyrqrIRNDLKKSSALIKKHTGRAPRVMVWPYGAYNGTLIEEAA 161
                        170       180       190
                 ....*....|....*....|....*....|..
gi 446800108 243 KAGLKYGFSLEEKAVTPNSNDYYIPRILISDD 274
Cdd:cd10964  162 KLGMQLTFTLEDGANNADQSLSSIPRILVENN 193
CE4_DAC_u4_5s cd10973
Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide ...
114-274 2.21e-24

Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel; This family contains many uncharacterized bacterial polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213028 [Multi-domain]  Cd Length: 157  Bit Score: 96.19  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 114 RSVWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLdmiSKKELKEMYKTGLwEFETHTHDLHNLSKNnK 193
Cdd:cd10973    1 KTVVITIDDGYKSVYTNAFPILKKYGYPFTLFVYTEAIGRGYPDYL---SWDQIREMAKYGV-EIANHSYSHPHLVRL-G 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 194 SKLMKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSNDYYIPRILISD 273
Cdd:cd10973   76 EKMQEQWLEWIRQDIEKSQQRFEKELGKKPKLFAYPYGEYNPAIIKLVKEAGFEAAFQQSGGVVSAGTDLTALPRFPLSG 155

                 .
gi 446800108 274 D 274
Cdd:cd10973  156 D 156
CE4_DAC_u1_6s cd10970
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
116-283 9.52e-24

Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 6-stranded beta/alpha barrel; This family contains uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213027 [Multi-domain]  Cd Length: 194  Bit Score: 95.46  E-value: 9.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 116 VWINFDDMDETIYENAYPILKKYKIPATGFIITGHVGEENFHNLDmiskkELKEMYKTGlWEFETHTHDlHnlsknnkSK 195
Cdd:cd10970    3 VSLTFDDGYESQYTTAFPILQEYGIPATAAVIPDSIGSSGRLTLD-----QLRELQDAG-WEIASHTLT-H-------TD 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 196 LMKSSEATIIKDLNKSEKYLTKN-FKKSQKTIAYPYGLMNDDKLPVIKK---AGLKYGFSLEEkavTPNSNDYYIPRILI 271
Cdd:cd10970   69 LTELSADEQRAELTESKRWLEDNgFGDGADHFAYPYGRYDDEVLELVREyydLGRSGGGGPNG---RPPLDPYRLRRVTG 145
                        170
                 ....*....|..
gi 446800108 272 SDDAFEHLIKRW 283
Cdd:cd10970  146 EADTTTEEVKTL 157
hmsF PRK14581
outer membrane N-deacetylase; Provisional
34-274 1.62e-16

outer membrane N-deacetylase; Provisional


Pssm-ID: 184753 [Multi-domain]  Cd Length: 672  Bit Score: 79.64  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  34 PPKKLKYKENSALALNYHRVRkanflnnfiyffSSSKEIKNYSVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGK-FP 112
Cdd:PRK14581  38 PQSERPWQKNTFVVIAYHDVE------------DDSADQRYLSVRSSALNEQFVWLRDNGYHVVSVDQILAARNGGPtLP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 113 KRSVWINFDDMDETIYENAYPILKKYKIPA----TGFIITGHVGEE-NFHNLD-----MISKKELKEMYKTGLWEFETHT 182
Cdd:PRK14581 106 DKAVLLTFDDGYSSFYRRVYPLLKAYKWSAvlapVGTWIDTATDKKvDFGGLStdrdrFATWKQITEMSKSGLVEIGAHT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 183 HDLH----------------NLSKNNKSKLMKSSEA---TIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKK 243
Cdd:PRK14581 186 YASHygvianpqgntepaaaNLQYDPKTKQYETVEAfkqRMEKDVALITQRIVQATGKQPRVWVWPYGAPNGTVLNILRQ 265
                        250       260       270
                 ....*....|....*....|....*....|..
gi 446800108 244 AGLKYGFSLEEKAVtpNSNDYY-IPRILISDD 274
Cdd:PRK14581 266 HGYQLAMTLDPGVA--NINDLMnIPRILISNN 295
pgaB PRK14582
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB;
34-274 1.21e-13

poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB;


Pssm-ID: 184754 [Multi-domain]  Cd Length: 671  Bit Score: 70.95  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108  34 PPKKLKYKENSALALNYHRVRKANFLNNFIyffssskeiknySVSQSQFESQIKWLKSHDAKFLTLKEFLYYKKKGK-FP 112
Cdd:PRK14582  38 LLAEQPWPHNGFVAIAYHDVEDEAADQRFM------------SVRTSALREQFAWLRENGYQPVSVAQILEAHRGGKpLP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 113 KRSVWINFDDMDETIYENAYPILKKYKIPA----TGFIITGHVGEE-NFHNL-----DMISKKELKEMYKTGLWEFETHT 182
Cdd:PRK14582 106 EKAVLLTFDDGYSSFYTRVFPILQAFQWPAvwapVGSWVDTPADQPvKFGGEmvpreYFATWQQVREVARSRLVEIASHT 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 183 HDLHNLSKNNKSKLMKSSEAT-------------------IIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKK 243
Cdd:PRK14582 186 WNSHYGIQANPQGSLLPAAVNrayftdharyetaaeyrerIRLDAVKMTEYIRTKAGKNPRVWVWPYGEANGIALEELKK 265
                        250       260       270
                 ....*....|....*....|....*....|.
gi 446800108 244 AGLKYGFSLEEkAVTPNSNDYYIPRILISDD 274
Cdd:PRK14582 266 LGYDMAFTLES-GLANASQLDSIPRVLIANN 295
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
118-243 3.47e-09

Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is represented by the extracellular polysaccharide-degrading enzyme, gellan lyase (gellanase, EC 4.2.2.-), from Bacillus sp. The enzyme acts on gellan exolytically and releases a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminus. The family also includes many uncharacterized prokaryotic polysaccharide deacetylases, which show high sequence similarity to Bacillus sp. gellan lyase. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200589 [Multi-domain]  Cd Length: 202  Bit Score: 55.46  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 118 INFDDMDETIYEnAYPILKKYKIPATGFIITGHVGEENFHNLDmiskkELKEMYKTGlWEFETHTHDLHNLSknnksklm 197
Cdd:cd10967    5 LTFDDGYAQDLR-AAPLLAKYGLKGTFFVNSGLLGRRGYLDLE-----ELRELAAAG-HEIGSHTVTHPDLT-------- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446800108 198 KSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKK 243
Cdd:cd10967   70 SLPPAELRREIAESRAALEEIGGFPVTSFAYPFGSTNPSIVPLLAR 115
CE4_SmPgdA_like cd10944
Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, ...
134-250 8.76e-08

Catalytic NodB homology domain of Streptococcus mutans polysaccharide deacetylase PgdA, Bacillus subtilis YheN, and similar proteins; This family is represented by a putative polysaccharide deacetylase PgdA from the oral pathogen Streptococcus mutans (SmPgdA) and Bacillus subtilis YheN (BsYheN), which are members of the carbohydrate esterase 4 (CE4) superfamily. SmPgdA is an extracellular metal-dependent polysaccharide deacetylase with a typical CE4 fold, with metal bound to a His-His-Asp triad. It possesses de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. SmPgdA plays a role in tuning cell surface properties and in interactions with (salivary) agglutinin, an essential component of the innate immune system, most likely through deacetylation of an as-yet-unidentified polysaccharide. SmPgdA shows significant homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae (SpPgdA) and Listeria monocytogenes (LmPgdA), both of which are involved in the bacterial defense mechanism against human mucosal lysozyme. The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. The biological function of BsYheN is still unknown. This family also includes many uncharacterized polysaccharide deacetylases mainly found in bacteria.


Pssm-ID: 200569 [Multi-domain]  Cd Length: 189  Bit Score: 51.39  E-value: 8.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 134 ILKKYKIPATGFIItGHVGEENfhnldmisKKELKEMYKTGlwefetHTHDLHNLSkNNKSKLMKSSEAtIIKDLNKSEK 213
Cdd:cd10944   21 ILKKYNVKATFFVI-GSNVEKY--------PELVKRIVKEG------HAIGLHSYT-HDYKKLYSSPEA-FIKDLNKTQD 83
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446800108 214 YLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKYGF 250
Cdd:cd10944   84 LIKKITGVKTKLIRFPGGSSNTGLMKALRKALTKRGY 120
CE4_SF cd10585
Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate ...
115-236 5.52e-07

Catalytic NodB homology domain of the carbohydrate esterase 4 superfamily; The carbohydrate esterase 4 (CE4) superfamily mainly includes chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan, respectively. Members in this superfamily contain a NodB homology domain that adopts a deformed (beta/alpha)8 barrel fold, which encompasses a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad, closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The NodB homology domain of CE4 superfamily is remotely related to the 7-stranded beta/alpha barrel catalytic domain of the superfamily consisting of family 38 glycoside hydrolases (GH38), family 57 heat stable retaining glycoside hydrolases (GH57), lactam utilization protein LamB/YcsF family proteins, and YdjC-family proteins.


Pssm-ID: 213020 [Multi-domain]  Cd Length: 142  Bit Score: 48.21  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 115 SVWINFDDMDETIYENA-----YPILKKYKIPATGFIITGHVGEENFHNLDMIsKKELKEMYKTGlWEFETHTHDLHNLS 189
Cdd:cd10585    1 LVLLTLDDDPAFEGSPAalqrlLDLLEGYGIPATLFVIPGNANPDKLMKSPLN-WDLLRELLAYG-HEIGLHGYTHPDLA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446800108 190 KNNksklmkSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDD 236
Cdd:cd10585   79 YGN------LSPEEVLEDLLRARRILEEAGGQPPKGFRAPGGNLSET 119
CE4_DAC_u2_5s cd10971
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
152-269 7.56e-07

Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel; This family contains many uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of this family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200593 [Multi-domain]  Cd Length: 198  Bit Score: 48.46  E-value: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 152 GEENFHNLDMiSKKELKEMYKTGLwEFETHTHDlHNLsknnkskLMKSSEATIIKDLNKSEKYLTK-NFKKSQKTIAYPY 230
Cdd:cd10971   83 EEAFAKELYM-TKDQIKQLERAGM-HIGSHGYD-HYW-------LGRLSPEEQEAEIKKSLKFLSEvGGGHDRWTFCYPY 152
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446800108 231 GLMNDDKLPVIKKAGLKYGFSLEEKAVTPNSND-YYIPRI 269
Cdd:cd10971  153 GSFNEETLEILKENGCRLGFTTEVAIADLDDLEpLELPRY 192
CE4_Mlr8448_like_5s cd10968
Putative catalytic NodB homology domain of Mesorhizobium loti Mlr8448 protein and its ...
114-272 4.12e-06

Putative catalytic NodB homology domain of Mesorhizobium loti Mlr8448 protein and its bacterial homologs; This family contains Mesorhizobium loti Mlr8448 protein and its bacterial homologs. Although their biochemical properties are yet to be determined, members in this subfamily contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213025 [Multi-domain]  Cd Length: 161  Bit Score: 46.09  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 114 RSVWINFDDMDETIYENAYPILKKYKIPATGFIITG---HVGEENFHNLDMISKKELKEMYKTGLWEFETHTHDLHNLSk 190
Cdd:cd10968    1 RFAVLTFDDGYRDNLEFALPVFERHGVPFTIYVTTGfpdGTGELWWLTLECLDWDELRRLAADPLVTIGAHTITHPNLA- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 191 nnksklmKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGL---MNDDKLPVIKKAGLKYGFSLEEKAVTPNSND--YY 265
Cdd:cd10968   80 -------RLSDDEARREIAASRARLEAELGREVRHFAYPYGDrtaAGPREADLAREAGFATAVTTRPGVLFAEHREnlHA 152

                 ....*..
gi 446800108 266 IPRILIS 272
Cdd:cd10968  153 LPRISLN 159
CE4_NodB_like_6s_7s cd10917
Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the ...
114-248 2.96e-05

Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.


Pssm-ID: 213022 [Multi-domain]  Cd Length: 171  Bit Score: 43.76  E-value: 2.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 114 RSVWINFDDMDETIYENAY-PILKKYKIPATGFIITGHVGEenfhNLDMIskkelKEMYKTGlwefethtHDLHNLSKNN 192
Cdd:cd10917    1 KVVALTFDDGPDPEYTPKIlDILAEYGVKATFFVVGENVEK----HPDLV-----RRIVAEG--------HEIGNHTYSH 63
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446800108 193 KSkLMKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDDKLPVIKKAGLKY 248
Cdd:cd10917   64 PD-LTKLSPEEIRAEIERTQDAIEEATGVRPRLFRPPYGAYNPEVLAAAAELGLTV 118
CE4_SpPgdA_BsYjeA_like cd10947
Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, ...
114-236 1.07e-04

Catalytic NodB homology domain of Streptococcus pneumoniae peptidoglycan deacetylase PgdA, Bacillus subtilis BsYjeA protein, and their bacterial homologs; This family is represented by Streptococcus pneumoniae peptidoglycan GlcNAc deacetylase (SpPgdA), a member of the carbohydrate esterase 4 (CE4) superfamily. SpPgdA protects gram-positive bacterial cell wall from host lysozymes by deacetylating peptidoglycan N-acetylglucosamine (GlcNAc) residues. It consists of three separate domains: N-terminal, middle and C-terminal (catalytic) domains. The catalytic NodB homology domain is similar to the deformed (beta/alpha)8 barrel fold adopted by other CE4 esterases, which harbors a mononuclear metalloenzyme employing a conserved His-His-Asp zinc-binding triad closely associated with conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. The enzyme is able to accept GlcNAc3 as a substrate, with the N-acetyl of the middle sugar being removed by the enzyme. This family also includes Bacillus subtilis BsYjeA protein encoded by the yjeA gene, which is one of the six polysaccharide deacetylase gene homologs (pdaA, pdaB/ybaN, yheN, yjeA, yxkH and ylxY) in the Bacillus subtilis genome. Although homology comparison shows that the BsYjeA protein contains a polysaccharide deacetylase domain, and was predicted to be a membrane-bound xylanase or a membrane-bound chitooligosaccharide deacetylase, more recent research indicates BsYjeA might be a novel non-specific secretory endonuclease which creates random nicks progressively on the two strands of dsDNA, resulting in highly distinguishable intermediates/products very different in chemical and physical compositions over time. In addition, BsYjeA shares several enzymatic properties with the well-understood DNase I endonuclease. Both enzymes are active on ssDNA and dsDNA, both generate random nicks, and both require Mg2+ or Mn2+ for hydrolytic activity.


Pssm-ID: 200571 [Multi-domain]  Cd Length: 177  Bit Score: 41.99  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 114 RSVWINFDD-MDETIYENAYPILKKYKIPATGFIITGHVgeENFHNLdmiskkeLKEMYKTGlWEFETHTHDLHNLSknn 192
Cdd:cd10947    1 KVVALTFDDgPDPTTTPQVLKTLKKYKAPATFFMLGSNV--KTYPEL-------VRRVLDAG-HEIGNHSWSHPQLT--- 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446800108 193 ksklmKSSEATIIKDLNKSEKYLTKNFKKSQKTIAYPYGLMNDD 236
Cdd:cd10947   68 -----KLSVAEAEKQINDTDDAIEKATGNRPTLLRPPYGATNRS 106
CE4_GT2-like cd10962
Catalytic NodB homology domain of uncharacterized bacterial glycosyl transferase, group 2-like ...
114-248 4.10e-03

Catalytic NodB homology domain of uncharacterized bacterial glycosyl transferase, group 2-like family proteins; This family includes many uncharacterized bacterial proteins containing an N-terminal GH18 (glycosyl hydrolase, family 18) domain, a middle NodB-like homology domain, and a C-terminal GT2-like (glycosyl transferase group 2) domain. Although their biological function is unknown, members in this family contain a middle NodB homology domain that is similar to the catalytic domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily. The presence of three domains suggests that members of this family may be multifunctional.


Pssm-ID: 200584 [Multi-domain]  Cd Length: 196  Bit Score: 37.66  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446800108 114 RSVWINFDD-MDETIYENAYPILKKYKIPATGFIItghvGEENFHNLDMiskkeLKEMYKTGlWEFETHTHDLHNLSKNn 192
Cdd:cd10962    1 KKIALTFDDgPDPEWTPQILDILKEYQIPATFFVI----GENAVNNPEL-----VKRIIDEG-HEIGNHTFTHPDLDLL- 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446800108 193 ksklmksSEATIIKDLNKSEKYLTKNFKKSqkTIAY--PYG-----LMNDDKLPVIKKAGLKY 248
Cdd:cd10962   70 -------SEKRTRLELNATQRLIEAATGHS--TLLFrpPYGadanpTSADEIAPILKAQDRGY 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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