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Conserved domains on  [gi|1186201091|ref|WP_085398018|]
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polysaccharide deacetylase family protein [Salmonella enterica]

Protein Classification

polysaccharide deacetylase family protein( domain architecture ID 10181070)

polysaccharide deacetylase family protein belonging to the carbohydrate esterase 4 (CE4) superfamily, may catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan

CATH:  3.20.20.370
CAZY:  CE4
EC:  3.-.-.-
PubMed:  12644381
SCOP:  3001025

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CE4_Ecf1_like_5s cd10969
Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli ...
26-254 2.11e-80

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: 241.42  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  26 PETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPVR 104
Cdd:cd10969     1 PETFEEQLKYLKKNGYRTLSLEELLAFLKGGKpLPKKSVLITFDDGYLDNYVYAYPILKKYGLKATIFVVTGFIDEASGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 105 FSQKNEY---SHRDCEQRIAQGYADDVMLRWSEVNEMLRSDLVEFHVHTHSHTRWdkmfssrqeqcrhlRQDILEGKICL 181
Cdd:cd10969    81 RPTLFDYwsgDMPEANKIFFLKGRDEVFLSWEELREMEDSGVFDIQSHSHSHTRV--------------EYELEESKRLL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1186201091 182 AEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYLYTTERRMNCPANGTLRLGRISTKERENSaWLKRRLFCYT 254
Cdd:cd10969   147 EENLGKKVDHFCWPWGHYSPESLRIAKELGFKFFFTTKKGVNVPGEDPDRIKRITVKKDGGF-WLKKRLFLFS 218
 
Name Accession Description Interval E-value
CE4_Ecf1_like_5s cd10969
Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli ...
26-254 2.11e-80

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: 241.42  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  26 PETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPVR 104
Cdd:cd10969     1 PETFEEQLKYLKKNGYRTLSLEELLAFLKGGKpLPKKSVLITFDDGYLDNYVYAYPILKKYGLKATIFVVTGFIDEASGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 105 FSQKNEY---SHRDCEQRIAQGYADDVMLRWSEVNEMLRSDLVEFHVHTHSHTRWdkmfssrqeqcrhlRQDILEGKICL 181
Cdd:cd10969    81 RPTLFDYwsgDMPEANKIFFLKGRDEVFLSWEELREMEDSGVFDIQSHSHSHTRV--------------EYELEESKRLL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1186201091 182 AEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYLYTTERRMNCPANGTLRLGRISTKERENSaWLKRRLFCYT 254
Cdd:cd10969   147 EENLGKKVDHFCWPWGHYSPESLRIAKELGFKFFFTTKKGVNVPGEDPDRIKRITVKKDGGF-WLKKRLFLFS 218
deacetyl_PgaB TIGR03938
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems ...
5-235 2.77e-33

poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems produce polysaccharide based on N-acetyl-D-glucosamine in straight chains with beta-1,6 linkages. These are encoded by the icaADBC operon in Staphylococcus species, where the system is designated polysaccharide intercellular adhesin (PIA), and the pgaABCD operon in Gram-negative bacteria such as E. coli. Both systems include a putative polysaccharide deacetylase. The PgaB protein, described here, contains an additional domain lacking from its Gram-positive counterpart IcaB (TIGR03933). Deacetylation by this protein appears necessary to allow export through the porin PgaA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274867  Cd Length: 619  Bit Score: 127.43  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091   5 KHLPVLMYHHI---SRC-PGLVTLSPETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVY 79
Cdd:TIGR03938   1 NTFVVLCYHDVrddSAAdQDPYAVSTDALIEHFNWLRQNGYHPVSVDQILDARRGGKpLPEKAVLLTFDDGYRSFYTRVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  80 PVLKEFNLRAHIFLITGLI---GDGPVRFSQKNeyshrdceqriaqgYADDVMLRWSEVNEMLRSDLVEFHVHTH-SH-- 153
Cdd:TIGR03938  81 PLLKAYNYPAVLALVGSWLdtpANQKVDYGGEK--------------LPRDRFLTWEQIREMQASGLVEIASHTYdLHhg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 154 --------------TR-WD---KMFSSRQEQCRHLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYL 215
Cdd:TIGR03938 147 ilanpqgnelpaatTRaYDpatGRYETDAEYRQRIRDDLKKSSALIKKYTGKAPRVMVWPYGAYNGTAIKIAKELGMPVA 226
                         250       260
                  ....*....|....*....|
gi 1186201091 216 YTTERRMNCPANGTLRLGRI 235
Cdd:TIGR03938 227 LTLDDGPNTVDDPLNALRRI 246
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
55-214 1.18e-27

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: 103.08  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  55 GGKLPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPvrfsqkneyshrdceqriaqgyaddvmlrwSE 134
Cdd:pfam01522   1 KGPTPKKVVALTFDDGPSENTPAILDVLKKYGVKATFFVIGGNVERYP------------------------------DL 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 135 VNEMLRSDlVEFHVHTHSHTRWDKMFSSRQeqcrhlRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSY 214
Cdd:pfam01522  51 VKRMVEAG-HEIGNHTWSHPNLTGLSPEEI------RKEIERAQDALEKATGKRPRLFRPPYGSYNDTVLEVAKKLGYTA 123
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
43-218 2.18e-24

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: 96.65  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  43 TVTSDDMEFFYQGGKLPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPvrfsqkneyshrdceqriaq 122
Cdd:COG0726     2 VLSLDELLPALRWGPLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVERHP-------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 123 gyaddvmlrwSEVNEMLRSDlVEFHVHTHSHTRWDKMfsSRQEQcrhlRQDILEGKICLAEKTGKYSRHLCWPEGYYNVD 202
Cdd:COG0726    62 ----------ELVREIAAAG-HEIGNHTYTHPDLTKL--SEEEE----RAEIARAKEALEELTGKRPRGFRPPYGRYSPE 124
                         170
                  ....*....|....*.
gi 1186201091 203 YIQVAEELGFSYLYTT 218
Cdd:COG0726   125 TLDLLAELGYRYILWD 140
pgaB PRK14582
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB;
4-219 2.43e-24

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


Pssm-ID: 184754 [Multi-domain]  Cd Length: 671  Bit Score: 102.15  E-value: 2.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091   4 AKHLPVLMYHHIS-RCPG--LVTLSPETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVY 79
Cdd:PRK14582   46 HNGFVAIAYHDVEdEAADqrFMSVRTSALREQFAWLRENGYQPVSVAQILEAHRGGKpLPEKAVLLTFDDGYSSFYTRVF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  80 PVLKEFNLRAHIFLITGLI---GDGPVRFSqkneyshrdcEQRIAQGYaddvMLRWSEVNEMLRSDLVEFHVHT-HSHT- 154
Cdd:PRK14582  126 PILQAFQWPAVWAPVGSWVdtpADQPVKFG----------GEMVPREY----FATWQQVREVARSRLVEIASHTwNSHYg 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 155 ----------------RWD---KMFSSRQEQCRHLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYL 215
Cdd:PRK14582  192 iqanpqgsllpaavnrAYFtdhARYETAAEYRERIRLDAVKMTEYIRTKAGKNPRVWVWPYGEANGIALEELKKLGYDMA 271

                  ....
gi 1186201091 216 YTTE 219
Cdd:PRK14582  272 FTLE 275
 
Name Accession Description Interval E-value
CE4_Ecf1_like_5s cd10969
Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli ...
26-254 2.11e-80

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: 241.42  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  26 PETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPVR 104
Cdd:cd10969     1 PETFEEQLKYLKKNGYRTLSLEELLAFLKGGKpLPKKSVLITFDDGYLDNYVYAYPILKKYGLKATIFVVTGFIDEASGV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 105 FSQKNEY---SHRDCEQRIAQGYADDVMLRWSEVNEMLRSDLVEFHVHTHSHTRWdkmfssrqeqcrhlRQDILEGKICL 181
Cdd:cd10969    81 RPTLFDYwsgDMPEANKIFFLKGRDEVFLSWEELREMEDSGVFDIQSHSHSHTRV--------------EYELEESKRLL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1186201091 182 AEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYLYTTERRMNCPANGTLRLGRISTKERENSaWLKRRLFCYT 254
Cdd:cd10969   147 EENLGKKVDHFCWPWGHYSPESLRIAKELGFKFFFTTKKGVNVPGEDPDRIKRITVKKDGGF-WLKKRLFLFS 218
CE4_NodB_like_5s_6s cd10918
Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a ...
62-235 1.34e-45

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: 150.44  E-value: 1.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  62 SVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPVrfsqkneyshrdceqRIAQGYADDVMLRWSEVNEMLRS 141
Cdd:cd10918     1 PVVLTFDDGYRDNYTYALPILKKYGLPATFFVITGYIGGGNP---------------WWAPAPPRPPYLTWDQLRELAAS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 142 dLVEFHVHTHSHTRWDKMfsSRQEqcrhLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYLYTTERR 221
Cdd:cd10918    66 -GVEIGSHTHTHPDLTTL--SDEE----LRRELAESKERLEEELGKPVRSFAYPYGRYNPRVIAALKEAGYKAAFTTDPG 138
                         170
                  ....*....|....
gi 1186201091 222 MNCPANGTLRLGRI 235
Cdd:cd10918   139 LNSPGDDPYALPRI 152
deacetyl_PgaB TIGR03938
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems ...
5-235 2.77e-33

poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems produce polysaccharide based on N-acetyl-D-glucosamine in straight chains with beta-1,6 linkages. These are encoded by the icaADBC operon in Staphylococcus species, where the system is designated polysaccharide intercellular adhesin (PIA), and the pgaABCD operon in Gram-negative bacteria such as E. coli. Both systems include a putative polysaccharide deacetylase. The PgaB protein, described here, contains an additional domain lacking from its Gram-positive counterpart IcaB (TIGR03933). Deacetylation by this protein appears necessary to allow export through the porin PgaA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274867  Cd Length: 619  Bit Score: 127.43  E-value: 2.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091   5 KHLPVLMYHHI---SRC-PGLVTLSPETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVY 79
Cdd:TIGR03938   1 NTFVVLCYHDVrddSAAdQDPYAVSTDALIEHFNWLRQNGYHPVSVDQILDARRGGKpLPEKAVLLTFDDGYRSFYTRVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  80 PVLKEFNLRAHIFLITGLI---GDGPVRFSQKNeyshrdceqriaqgYADDVMLRWSEVNEMLRSDLVEFHVHTH-SH-- 153
Cdd:TIGR03938  81 PLLKAYNYPAVLALVGSWLdtpANQKVDYGGEK--------------LPRDRFLTWEQIREMQASGLVEIASHTYdLHhg 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 154 --------------TR-WD---KMFSSRQEQCRHLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYL 215
Cdd:TIGR03938 147 ilanpqgnelpaatTRaYDpatGRYETDAEYRQRIRDDLKKSSALIKKYTGKAPRVMVWPYGAYNGTAIKIAKELGMPVA 226
                         250       260
                  ....*....|....*....|
gi 1186201091 216 YTTERRMNCPANGTLRLGRI 235
Cdd:TIGR03938 227 LTLDDGPNTVDDPLNALRRI 246
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
55-214 1.18e-27

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: 103.08  E-value: 1.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  55 GGKLPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPvrfsqkneyshrdceqriaqgyaddvmlrwSE 134
Cdd:pfam01522   1 KGPTPKKVVALTFDDGPSENTPAILDVLKKYGVKATFFVIGGNVERYP------------------------------DL 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 135 VNEMLRSDlVEFHVHTHSHTRWDKMFSSRQeqcrhlRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSY 214
Cdd:pfam01522  51 VKRMVEAG-HEIGNHTWSHPNLTGLSPEEI------RKEIERAQDALEKATGKRPRLFRPPYGSYNDTVLEVAKKLGYTA 123
CE4_PgaB_5s cd10964
N-terminal putative catalytic polysaccharide deacetylase domain of bacterial poly-beta-1, ...
58-235 4.44e-26

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: 101.27  E-value: 4.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  58 LPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIgDGPVrfSQKNEYSHRDceqriaqgYADDVMLRWSEVNE 137
Cdd:cd10964     1 LPAKAVLLTFDDGYQSFYTRVYPLLKAYKYPAVLALVGSWL-ETPA--GKKVDYGGEQ--------LPRDRFLSWEQIRE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 138 MLRSDLVEFHVHTH-SH----------------TRWDKMFSSRQEQCRHLRQDILEG-KI---CLAEKTGKYSRHLCWPE 196
Cdd:cd10964    70 MQASGLVEIASHSHdLHhgipanpqgnllpaatTRQYDPKTGRYETDAEYRQRIRNDlKKssaLIKKHTGRAPRVMVWPY 149
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1186201091 197 GYYNVDYIQVAEELGFSYLYTTERRMNCPANGTLRLGRI 235
Cdd:cd10964   150 GAYNGTLIEEAAKLGMQLTFTLEDGANNADQSLSSIPRI 188
CE4_yadE_5s cd10966
Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and ...
59-235 3.13e-25

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: 98.12  E-value: 3.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  59 PRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPVRFSQKNEYShrdceqriaqgyaddvmlrWSEVNEM 138
Cdd:cd10966     1 PEKSVVITFDDGYKSNYEYAYPILKKYGFKATIFVIGSRIGEKPQDPKILQYLS-------------------IEELKEM 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 139 lrSDLVEFHVHTHS-HTRWDK-----MFSSRQEqcrhLRQDILegkicLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGF 212
Cdd:cd10966    62 --RDVFEFQSHTYNmHRGGGTgghglLALSEEE----ILADLK-----KSEEILGSSKAFAYPYGDYNDNAIEALKEAGV 130
                         170       180
                  ....*....|....*....|...
gi 1186201091 213 SYLYTTERRMNCPANGTLRLGRI 235
Cdd:cd10966   131 KLAFTTNEGKVTPGDDPYELPRV 153
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
43-218 2.18e-24

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: 96.65  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  43 TVTSDDMEFFYQGGKLPRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPvrfsqkneyshrdceqriaq 122
Cdd:COG0726     2 VLSLDELLPALRWGPLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVERHP-------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 123 gyaddvmlrwSEVNEMLRSDlVEFHVHTHSHTRWDKMfsSRQEQcrhlRQDILEGKICLAEKTGKYSRHLCWPEGYYNVD 202
Cdd:COG0726    62 ----------ELVREIAAAG-HEIGNHTYTHPDLTKL--SEEEE----RAEIARAKEALEELTGKRPRGFRPPYGRYSPE 124
                         170
                  ....*....|....*.
gi 1186201091 203 YIQVAEELGFSYLYTT 218
Cdd:COG0726   125 TLDLLAELGYRYILWD 140
pgaB PRK14582
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB;
4-219 2.43e-24

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


Pssm-ID: 184754 [Multi-domain]  Cd Length: 671  Bit Score: 102.15  E-value: 2.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091   4 AKHLPVLMYHHIS-RCPG--LVTLSPETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVY 79
Cdd:PRK14582   46 HNGFVAIAYHDVEdEAADqrFMSVRTSALREQFAWLRENGYQPVSVAQILEAHRGGKpLPEKAVLLTFDDGYSSFYTRVF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  80 PVLKEFNLRAHIFLITGLI---GDGPVRFSqkneyshrdcEQRIAQGYaddvMLRWSEVNEMLRSDLVEFHVHT-HSHT- 154
Cdd:PRK14582  126 PILQAFQWPAVWAPVGSWVdtpADQPVKFG----------GEMVPREY----FATWQQVREVARSRLVEIASHTwNSHYg 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 155 ----------------RWD---KMFSSRQEQCRHLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYL 215
Cdd:PRK14582  192 iqanpqgsllpaavnrAYFtdhARYETAAEYRERIRLDAVKMTEYIRTKAGKNPRVWVWPYGEANGIALEELKKLGYDMA 271

                  ....
gi 1186201091 216 YTTE 219
Cdd:PRK14582  272 FTLE 275
CE4_DAC_u4_5s cd10973
Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide ...
61-220 1.29e-22

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: 90.79  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  61 KSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGdgpvrfsqkneyshrdceqriaQGYADdvMLRWSEVNEMlR 140
Cdd:cd10973     1 KTVVITIDDGYKSVYTNAFPILKKYGYPFTLFVYTEAIG----------------------RGYPD--YLSWDQIREM-A 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 141 SDLVEFHVHTHSHTRWDKMFSSRQEQCRH-LRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYLYTTE 219
Cdd:cd10973    56 KYGVEIANHSYSHPHLVRLGEKMQEQWLEwIRQDIEKSQQRFEKELGKKPKLFAYPYGEYNPAIIKLVKEAGFEAAFQQS 135

                  .
gi 1186201091 220 R 220
Cdd:cd10973   136 G 136
CE4_IcaB_5s cd10965
Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion ...
59-235 8.54e-19

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: 81.28  E-value: 8.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  59 PRKSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGdgpvrfsQKNEYSHrdceqriaqgyaddvMLRWSEVNEM 138
Cdd:cd10965     1 PGKYVVITFDDVDQTVYDNAFPILKKLKIPFTQFVITGQVG-------STNFGLN---------------LATWSQIKEM 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 139 LRSDLVEFHVHTHSHTRWDK-----MFSSRQEQcrhLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEELGFS 213
Cdd:cd10965    59 VASGLVTFGLHTNDLHYLVKdkkklFTPASYSR---FAEDYAKSQKCLKEKLGKKTRYFAYPYGEGNKDTQKILKKQGIQ 135
                         170       180
                  ....*....|....*....|..
gi 1186201091 214 YLYTTERRMNCPANGTLRLGRI 235
Cdd:cd10965   136 YGFTLRDKVVTNDSDNYRIPRI 157
hmsF PRK14581
outer membrane N-deacetylase; Provisional
9-219 2.55e-16

outer membrane N-deacetylase; Provisional


Pssm-ID: 184753 [Multi-domain]  Cd Length: 672  Bit Score: 78.48  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091   9 VLMYHHI---SRCPGLVTLSPETFREQMEWLAENNWKTVTSDDMEFFYQGGK-LPRKSVMLTFDDGYLDNWFHVYPVLKE 84
Cdd:PRK14581   51 VIAYHDVeddSADQRYLSVRSSALNEQFVWLRDNGYHVVSVDQILAARNGGPtLPDKAVLLTFDDGYSSFYRRVYPLLKA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  85 FNLRAhIFLITGLIGDGPVrfSQKNEYSHRDCEQriaqgyadDVMLRWSEVNEMLRSDLVEFHVHTHSH----------- 153
Cdd:PRK14581  131 YKWSA-VLAPVGTWIDTAT--DKKVDFGGLSTDR--------DRFATWKQITEMSKSGLVEIGAHTYAShygvianpqgn 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1186201091 154 -------TRWDKmfSSRQEQCRHLRQDILEGKICL-----AEKTGKYSRHLCWPEGYYNVDYIQVAEELGFSYLYTTE 219
Cdd:PRK14581  200 tepaaanLQYDP--KTKQYETVEAFKQRMEKDVALitqriVQATGKQPRVWVWPYGAPNGTVLNILRQHGYQLAMTLD 275
CE4_Mlr8448_like_5s cd10968
Putative catalytic NodB homology domain of Mesorhizobium loti Mlr8448 protein and its ...
61-248 1.40e-14

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: 69.58  E-value: 1.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  61 KSVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIgdgpvrfsqknEYSHRdceqriAQGYADDVMlRWSEVNEMLR 140
Cdd:cd10968     1 RFAVLTFDDGYRDNLEFALPVFERHGVPFTIYVTTGFP-----------DGTGE------LWWLTLECL-DWDELRRLAA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 141 SDLVEFHVHTHSHTRWDKMfsSRQEqcrhLRQDILEGKICLAEKTGKYSRHLCWPEGY-YNVD--YIQVAEELGFSYLYT 217
Cdd:cd10968    63 DPLVTIGAHTITHPNLARL--SDDE----ARREIAASRARLEAELGREVRHFAYPYGDrTAAGprEADLAREAGFATAVT 136
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1186201091 218 TerrmncpangtlRLGRISTKERENSAWLKR 248
Cdd:cd10968   137 T------------RPGVLFAEHRENLHALPR 155
CE4_DAC_u2_5s cd10971
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
62-221 9.33e-10

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: 56.93  E-value: 9.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  62 SVMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPV---------RFSQK--NEYSHRDCEQRIA----QGYAD 126
Cdd:cd10971     1 AILLTFDDGYKDHYTYVLPELEERGIQGSFFVPAKPVEEHKVldvnkihfiLFIKRllQYELPEKLRTEILdklfKKYVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 127 DVMLRWSEVNEMLRSDLVEFHV-------HTHSHTRWDKMfsSRQEQcrhlRQDIlEGKICLAEKTGKYSRH--LCWPEG 197
Cdd:cd10971    81 ISEEAFAKELYMTKDQIKQLERagmhigsHGYDHYWLGRL--SPEEQ----EAEI-KKSLKFLSEVGGGHDRwtFCYPYG 153
                         170       180
                  ....*....|....*....|....
gi 1186201091 198 YYNVDYIQVAEELGFSYLYTTERR 221
Cdd:cd10971   154 SFNEETLEILKENGCRLGFTTEVA 177
CE4_DAC_u1_6s cd10970
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
63-248 2.82e-09

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: 55.40  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  63 VMLTFDDGYLDNWFHVYPVLKEFNLRAHIFLITGLIGDGPVrfsqkneyshrdceqriaqgyaddvmLRWSEVNEMlRSD 142
Cdd:cd10970     3 VSLTFDDGYESQYTTAFPILQEYGIPATAAVIPDSIGSSGR--------------------------LTLDQLREL-QDA 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 143 LVEFHVHTHSHTRWDKMFSSRQeqcrhlRQDILEGKICLAE-KTGKYSRHLCWPEGYYNVDYIQVAEElgfsyLYTTERR 221
Cdd:cd10970    56 GWEIASHTLTHTDLTELSADEQ------RAELTESKRWLEDnGFGDGADHFAYPYGRYDDEVLELVRE-----YYDLGRS 124
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1186201091 222 MNCPANGT-----LRLGRIS----TKERENSAWLKR 248
Cdd:cd10970   125 GGGGPNGRppldpYRLRRVTgeadTTTEEVKTLLDR 160
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
61-218 3.59e-08

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: 52.38  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091  61 KSVMLTFDDGYlDNWFHVYPVLKEFNLRAHIFLITGLIGDGPvrfsqkneyshrdceqriaqgyaddvMLRWSEVNEmLR 140
Cdd:cd10967     1 LAVSLTFDDGY-AQDLRAAPLLAKYGLKGTFFVNSGLLGRRG--------------------------YLDLEELRE-LA 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186201091 141 SDLVEFHVHTHSH---TRWDKmfssrqeqcRHLRQDILEGKICLAEKTGKYSRHLCWPEGYYNVDYIQVAEElGFSYLYT 217
Cdd:cd10967    53 AAGHEIGSHTVTHpdlTSLPP---------AELRREIAESRAALEEIGGFPVTSFAYPFGSTNPSIVPLLAR-GFIAARG 122

                  .
gi 1186201091 218 T 218
Cdd:cd10967   123 V 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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