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Conserved domains on  [gi|1270732711|gb|ATP12164|]
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peptidase M23 [Bartonella henselae]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

EC:  3.4.24.-
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M23
PubMed:  36386627

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 265-390 1.97e-43

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 155.31  E-value: 1.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 265 ATGISKMRWPVRGRLLSQFGQKR-GTTMSRGIDIAVPEGSSVKAAENGIVIYAsDGLKELGNVVMIRHENNIITIYGCNS 343
Cdd:COG4942   249 AALKGKLPWPVSGRVVRRFGERDgGGGRNKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHGGGYLTLYAHLS 327

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1270732711 344 KLVVTRGQRIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPIKYL 390
Cdd:COG4942   328 SLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWL 374
nlpD super family cl35964
murein hydrolase activator NlpD;
90-390 5.18e-19

murein hydrolase activator NlpD;


The actual alignment was detected with superfamily member PRK10871:

Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 86.81  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  90 TAYNSPPQDGTSSPNSRIMGTppRNLGTLSRSQmrndplFRQNSYIVQTGDTLLSIARQRGVSVEALKLVNGIRSN-SIY 168
Cdd:PRK10871   27 SNTSNPPAPVSSVGNGRIVYN--RQYGNIPKGS------YSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 169 IGQVLMIPSGrtaetSNVRNNDWGASKQSLSQSQSASsirhKKYSSTEKAPITPKPSAQINRSNGEQNSSAQMSSLNYEK 248
Cdd:PRK10871   99 VGQTLQVGNA-----SGTPITGGNAITQADAAEQGVV----IKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 249 GVLDTVMNKDNGVTPQATG--------ISKMRWPVRGRLLSQFGQKRGTtmSRGIDIAVPEGSSVKAAENGIVIYASDGL 320
Cdd:PRK10871  170 TTVTAPVTAPTASTTEPTAsstststpISTWRWPTDGKVIENFSASEGG--NKGIDIAGSKGQAIIATADGRVVYAGNAL 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 321 KELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVKTpRVYFEVRENSLPVDPIKYL 390
Cdd:PRK10871  248 RGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSST-RLHFEIRYKGKSVNPLRYL 316
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 265-390 1.97e-43

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 155.31  E-value: 1.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 265 ATGISKMRWPVRGRLLSQFGQKR-GTTMSRGIDIAVPEGSSVKAAENGIVIYAsDGLKELGNVVMIRHENNIITIYGCNS 343
Cdd:COG4942   249 AALKGKLPWPVSGRVVRRFGERDgGGGRNKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHGGGYLTLYAHLS 327

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1270732711 344 KLVVTRGQRIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPIKYL 390
Cdd:COG4942   328 SLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWL 374
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 290-386 5.20e-32

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 116.49  E-value: 5.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 290 TMSRGIDIAVPEGSSVKAAENGIVIYASDgLKELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVK 369
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 1270732711 370 TPRVYFEVRENSLPVDP 386
Cdd:pfam01551  80 GPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 293-377 1.01e-26

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 101.90  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 293 RGIDIAVPEGSSVKAAENGIVIYASDGlKELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVKTPR 372
Cdd:cd12797     2 NGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 1270732711 373 VYFEV 377
Cdd:cd12797    81 LHFEI 85
PRK11637 PRK11637
AmiB activator; Provisional
 273-390 8.45e-21

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 93.22  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 273 WPVRGRLLSQFG-QKRGTTMSRGIDIAVPEGSSVKAAENGIVIYAsDGLKELGNVVMIRHENNIITIYGCNSKLVVTRGQ 351
Cdd:PRK11637  309 WPVRGPTLHRFGeQLQGELRWKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGA 387

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1270732711 352 RIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPIKYL 390
Cdd:PRK11637  388 QVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQPWL 426
nlpD PRK10871
murein hydrolase activator NlpD;
90-390 5.18e-19

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 86.81  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  90 TAYNSPPQDGTSSPNSRIMGTppRNLGTLSRSQmrndplFRQNSYIVQTGDTLLSIARQRGVSVEALKLVNGIRSN-SIY 168
Cdd:PRK10871   27 SNTSNPPAPVSSVGNGRIVYN--RQYGNIPKGS------YSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 169 IGQVLMIPSGrtaetSNVRNNDWGASKQSLSQSQSASsirhKKYSSTEKAPITPKPSAQINRSNGEQNSSAQMSSLNYEK 248
Cdd:PRK10871   99 VGQTLQVGNA-----SGTPITGGNAITQADAAEQGVV----IKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 249 GVLDTVMNKDNGVTPQATG--------ISKMRWPVRGRLLSQFGQKRGTtmSRGIDIAVPEGSSVKAAENGIVIYASDGL 320
Cdd:PRK10871  170 TTVTAPVTAPTASTTEPTAsstststpISTWRWPTDGKVIENFSASEGG--NKGIDIAGSKGQAIIATADGRVVYAGNAL 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 321 KELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVKTpRVYFEVRENSLPVDPIKYL 390
Cdd:PRK10871  248 RGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSST-RLHFEIRYKGKSVNPLRYL 316
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
70-178 5.18e-15

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.05  E-value: 5.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  70 IQSTELPPVEPVNDLSTYDNTAYNSPPQDGTSSPNSRIMGTPPRNLGTLSRSQMRNDPLFRQNS--YIVQTGDTLLSIAR 147
Cdd:COG1388    46 LSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPvtYTVKKGDTLWSIAR 125

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1270732711 148 QRGVSVEALKLVNGIRSNSIYIGQVLMIPSG 178
Cdd:COG1388   126 RYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 134-176 3.50e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 60.49  E-value: 3.50e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1270732711 134 YIVQTGDTLLSIARQRGVSVEALKLVNGIRSNSIYIGQVLMIP 176
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 133-175 8.66e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 56.72  E-value: 8.66e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1270732711 133 SYIVQTGDTLLSIARQRGVSVEALKLVNGIRSNS-IYIGQVLMI 175
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM smart00257
Lysin motif;
134-175 6.23e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 51.29  E-value: 6.23e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1270732711  134 YIVQTGDTLLSIARQRGVSVEALKLVNGI-RSNSIYIGQVLMI 175
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNIlDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 265-390 1.97e-43

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 155.31  E-value: 1.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 265 ATGISKMRWPVRGRLLSQFGQKR-GTTMSRGIDIAVPEGSSVKAAENGIVIYAsDGLKELGNVVMIRHENNIITIYGCNS 343
Cdd:COG4942   249 AALKGKLPWPVSGRVVRRFGERDgGGGRNKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHGGGYLTLYAHLS 327

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1270732711 344 KLVVTRGQRIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPIKYL 390
Cdd:COG4942   328 SLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWL 374
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 272-390 2.39e-38

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 136.64  E-value: 2.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 272 RWPVRGRLLSQFGQKR-----GTTMSRGIDIAVPEGSSVKAAENGIVIYASDGlKELGNVVMIRHENNIITIYGCNSKLV 346
Cdd:COG0739    72 AWPVKGRITSGFGYRRhpvtgRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWN-GGYGNLVIIDHGNGYTTLYAHLSSIL 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1270732711 347 VTRGQRIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPIKYL 390
Cdd:COG0739   151 VKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 290-386 5.20e-32

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 116.49  E-value: 5.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 290 TMSRGIDIAVPEGSSVKAAENGIVIYASDgLKELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVK 369
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 1270732711 370 TPRVYFEVRENSLPVDP 386
Cdd:pfam01551  80 GPHLHFEIRKNGKPVDP 96
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 262-391 3.46e-28

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 109.73  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 262 TPQATGISKMRWPVRGRLLSQFGQKrgTTMSR---------GIDIAVPEGSSVKAAENGIVIYASDGlKELGNVVMIRHE 332
Cdd:COG5821    60 KVTASTSNKFLKPVSGKITREFGED--LVYSKtlnewrthtGIDIAAKEGTPVKAAADGVVVEVGKD-PKYGITVVIDHG 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270732711 333 NNIITIYG-CNSKLVVTRGQRIRRGDEIAKSGVSGDVKT---PRVYFEVRENSLPVDPIKYLE 391
Cdd:COG5821   137 NGIKTVYAnLDSKIKVKVGQKVKKGQVIGKVGSTALFESsegPHLHFEVLKNGKPVDPMKYLK 199
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 293-377 1.01e-26

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 101.90  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 293 RGIDIAVPEGSSVKAAENGIVIYASDGlKELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVKTPR 372
Cdd:cd12797     2 NGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 1270732711 373 VYFEV 377
Cdd:cd12797    81 LHFEI 85
PRK11637 PRK11637
AmiB activator; Provisional
 273-390 8.45e-21

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 93.22  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 273 WPVRGRLLSQFG-QKRGTTMSRGIDIAVPEGSSVKAAENGIVIYAsDGLKELGNVVMIRHENNIITIYGCNSKLVVTRGQ 351
Cdd:PRK11637  309 WPVRGPTLHRFGeQLQGELRWKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGA 387

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1270732711 352 RIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPIKYL 390
Cdd:PRK11637  388 QVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQPWL 426
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 218-390 2.90e-19

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 85.43  E-value: 2.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 218 APITPKPSAQINRSNGEQNSSAQMSSlNYEK------GVLDTVMNKDNGVTPQATGISkmrwPVRGRLLSQFGQKRgttm 291
Cdd:COG5833    50 SPPLEKAKAWVATVLTEEFQFAAVNQ-WYEEtfggplAFLPPFGKEEETVEQGEAFAL----PVSGKVVESFQENG---- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 292 sRGIDIAVPEGSSVKAAENGIVIYASDGlKELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSgDVKTP 371
Cdd:COG5833   121 -KGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPAT-EGEEG 197

                         170
                  ....*....|....*....
gi 1270732711 372 RVYFEVRENSLPVDPIKYL 390
Cdd:COG5833   198 TFYFAIKKGGKFIDPIQVI 216
nlpD PRK10871
murein hydrolase activator NlpD;
90-390 5.18e-19

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 86.81  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  90 TAYNSPPQDGTSSPNSRIMGTppRNLGTLSRSQmrndplFRQNSYIVQTGDTLLSIARQRGVSVEALKLVNGIRSN-SIY 168
Cdd:PRK10871   27 SNTSNPPAPVSSVGNGRIVYN--RQYGNIPKGS------YSGSTYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 169 IGQVLMIPSGrtaetSNVRNNDWGASKQSLSQSQSASsirhKKYSSTEKAPITPKPSAQINRSNGEQNSSAQMSSLNYEK 248
Cdd:PRK10871   99 VGQTLQVGNA-----SGTPITGGNAITQADAAEQGVV----IKPAQNSTVAVASQPTITYSESSGEQSANKMLPNNKPAA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 249 GVLDTVMNKDNGVTPQATG--------ISKMRWPVRGRLLSQFGQKRGTtmSRGIDIAVPEGSSVKAAENGIVIYASDGL 320
Cdd:PRK10871  170 TTVTAPVTAPTASTTEPTAsstststpISTWRWPTDGKVIENFSASEGG--NKGIDIAGSKGQAIIATADGRVVYAGNAL 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 321 KELGNVVMIRHENNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVKTpRVYFEVRENSLPVDPIKYL 390
Cdd:PRK10871  248 RGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSST-RLHFEIRYKGKSVNPLRYL 316
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
70-178 5.18e-15

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 72.05  E-value: 5.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  70 IQSTELPPVEPVNDLSTYDNTAYNSPPQDGTSSPNSRIMGTPPRNLGTLSRSQMRNDPLFRQNS--YIVQTGDTLLSIAR 147
Cdd:COG1388    46 LSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAAAAPSPvtYTVKKGDTLWSIAR 125

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1270732711 148 QRGVSVEALKLVNGIRSNSIYIGQVLMIPSG 178
Cdd:COG1388   126 RYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
PRK11649 PRK11649
putative peptidase; Provisional
 264-387 9.23e-15

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 75.47  E-value: 9.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 264 QATGISK--MRWPV--RGRLLSQFGQKRGTTMS------RGIDIAVPEGSSVKAAENGIVIYAS-DGlkELGNVVMIRHE 332
Cdd:PRK11649  275 NGSGLAKgfLRFPTakQFRISSNFNPRRLNPVTgrvaphRGVDFAMPVGTPVLAVGDGEVVVAKrSG--AAGNYVAIRHG 352

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1270732711 333 NNIITIYGCNSKLVVTRGQRIRRGDEIAKSGVSGDVKTPRVYFEVRENSLPVDPI 387
Cdd:PRK11649  353 RQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 134-176 3.50e-12

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 60.49  E-value: 3.50e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1270732711 134 YIVQTGDTLLSIARQRGVSVEALKLVNGIRSNSIYIGQVLMIP 176
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 133-175 8.66e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 56.72  E-value: 8.66e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1270732711 133 SYIVQTGDTLLSIARQRGVSVEALKLVNGIRSNS-IYIGQVLMI 175
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM smart00257
Lysin motif;
134-175 6.23e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 51.29  E-value: 6.23e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1270732711  134 YIVQTGDTLLSIARQRGVSVEALKLVNGI-RSNSIYIGQVLMI 175
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNIlDPDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 91-189 9.79e-08

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 53.59  E-value: 9.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  91 AYNSPPQDGTSSPNS--RIMgTPPRNLGTLSRS------------QMRNDPLFRQNSYIVQTGDTLLSIARQRGVSVEAL 156
Cdd:PRK10783  290 TFNAGYKRSTTAPSGphYIM-VPKKHADQLRESlasgeiaavqstLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDL 368

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1270732711 157 KLVNGIRSNSIYIGQVLMIPSGRTAETSNVRNN 189
Cdd:PRK10783  369 QQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSD 401
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
81-185 1.63e-07

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 53.16  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  81 VNDL-STYDNTAYNSPPQDGTSSPNSrimGTPPRNLGTLSRSQMRndplfrqnSYIVQTGDTLLSIARQRGVSVEALKLV 159
Cdd:PRK06347  290 LNDLiSRYNLTQYDSGKTTGGNSGST---GNSSNSSNTGNTSNAK--------IYTVVKGDSLWRIANNHKVTVANLKAW 358

                          90       100
                  ....*....|....*....|....*.
gi 1270732711 160 NGIRSNSIYIGQVLMIPSGRTAETSN 185
Cdd:PRK06347  359 NNLKSDFIYPGQKLKVSAGSTTSDTN 384
PRK13914 PRK13914
invasion associated endopeptidase;
77-262 5.31e-05

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 45.18  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711  77 PVEPVNDLSTYDNTAYNSPPQDGTSSPNSRIMGTPPRNlgtlSRSQMRNDPLFRQN--SYIVQTGDTLLSIARQRGVSVE 154
Cdd:PRK13914  147 PVAPTQEVKKETTTQQAAPAAETKTEVKQTTQATTPAP----KVAETKETPVVDQNatTHAVKSGDTIWALSVKYGVSVQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270732711 155 ALKLVNGIRSNSIYIGQVLMI--PSGRTAETSNVRNN----DWGASKQSLSQSQSASSIRHKKYSSTE-----KAPI--- 220
Cdd:PRK13914  223 DIMSWNNLSSSSIYVGQKLAIkqTANTATPKAEVKTEapaaEKQAAPVVKENTNTNTATTEKKETTTQqqtapKAPTeaa 302

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1270732711 221 --TPKPSAQINRSNGEQNSSAQMSSLNYEKGVLDTVMNKDNGVT 262
Cdd:PRK13914  303 kpAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTN 346
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
134-185 6.87e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 45.07  E-value: 6.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1270732711 134 YIVQTGDTLLSIARQRGVSVEALKLVNGIRSNSIYIGQVLMIPSGRTAETSN 185
Cdd:PRK06347  482 YTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTN 533
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
134-184 1.78e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 43.53  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270732711 134 YIVQTGDTLLSIARQRGVSVEALKLVNGIRSNSIYIGQVLMIPSGRTAETS 184
Cdd:PRK06347  408 YTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTN 458
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
133-175 1.83e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 43.53  E-value: 1.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1270732711 133 SYIVQTGDTLLSIARQRGVSVEALKLVNGIRSNSIYIGQVLMI 175
Cdd:PRK06347  549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 133-176 6.71e-04

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 39.99  E-value: 6.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1270732711 133 SYIVQTGDTLLSIARQR---GVSVEALKLVN--GIRS-NSIYIGQVLMIP 176
Cdd:COG1652   111 TYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNpDLIYPGQVLRIP 160
PRK13914 PRK13914
invasion associated endopeptidase;
132-182 1.24e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 40.94  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1270732711 132 NSYIVQTGDTLLSIARQRGVSVEALKLVNGIRSNSIYIGQVLMIPSGRTAE 182
Cdd:PRK13914   28 STVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAE 78
 
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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