ID W9AC29_9BACI Unreviewed; 673 AA.
AC W9AC29;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN Name=pbp {ECO:0000313|EMBL:CDO03284.1};
GN ORFNames=BN988_01790 {ECO:0000313|EMBL:CDO03284.1};
OS Oceanobacillus picturae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO03284.1, ECO:0000313|Proteomes:UP000028863};
RN [1] {ECO:0000313|EMBL:CDO03284.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO03284.1,
RC ECO:0000313|Proteomes:UP000028863};
RA Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequencing of Oceanobacillus picturae strain S1 isolated from
RT human gut.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDO03284.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO03284.1,
RC ECO:0000313|Proteomes:UP000028863};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO03284.1}.
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DR EMBL; CCAX010000001; CDO03284.1; -; Genomic_DNA.
DR RefSeq; WP_036575162.1; NZ_CCAX010000001.1.
DR AlphaFoldDB; W9AC29; -.
DR STRING; 171693.BN988_01790; -.
DR eggNOG; COG0768; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000028863; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000028863};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..673
FT /note="serine-type D-Ala-D-Ala carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038660490"
FT DOMAIN 25..149
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 158..313
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 355..662
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 673 AA; 73852 MW; E63BA0B13A0C67E9 CRC64;
MKKITIALAA IIMVVLAGCS DDEVTPNERF DTYVKHWNEQ EFSDAYGMLS SESTETYPTE
EYVDRYNKIY EDLAISDLSI SFSKLEEEEL ETAMEEGTAT IPFEVAMESM AGPIEFDYEA
TLVQEGEEDE QNWYVQWDPG FIFPELKDGG EISIQSEAPT RGEILDRNQM PLAINDKVNE
IGIIPGKLGS NPEQSKEELS SLIGLSVDAI DEALNAAWVE PDLFVPLKKV PSTNDLSPLW
EIDGVAGREV TGRVYPAGEA AGQLVGYIGN ITAEELEEQE PGVYSANDMI GKRGLESLYE
EQLKGKKGTR IEVIKENQEP IVLAETPVEN GKNITLTIDV NVQESIFDSY EEDAGTAAAI
NPKTGETLAL VSSPSFDPNE ILYGTKANLW ETLQEDEQQP LLNRFSSTFA PGSALKPITS
AIGLKNGSID PDEGLEIDGL TWSNGKGWGD YAVRRVSESS GPVDLKDALV RSDNIYFAMQ
AVNMGSEAYV KGLKEFGFGE DLPYEYPFTA SSISSDGKLD DEVLLANSSY GQGQLEMSSL
HLATAYTTFL NEGNMIKPTL LTSEETAQVW KENLLDNDQA NLMKDLLYEV GQSGTPSKYT
ADSEVGISGK TGTAELKLTT EDDSGEENGW FVGFPTKESE QDLLIAMMVE NVKEKGGSVY
TTKKVVDVFN ELK
//
