ID W9A7W4_9BACI Unreviewed; 695 AA.
AC W9A7W4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=pbpH {ECO:0000313|EMBL:CDO01884.1};
GN ORFNames=BN988_00336 {ECO:0000313|EMBL:CDO01884.1};
OS Oceanobacillus picturae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=171693 {ECO:0000313|EMBL:CDO01884.1, ECO:0000313|Proteomes:UP000028863};
RN [1] {ECO:0000313|EMBL:CDO01884.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO01884.1,
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:CDO01884.1, ECO:0000313|Proteomes:UP000028863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1 {ECO:0000313|EMBL:CDO01884.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:CDO01884.1}.
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DR EMBL; CCAX010000001; CDO01884.1; -; Genomic_DNA.
DR RefSeq; WP_036572573.1; NZ_CCAX010000001.1.
DR AlphaFoldDB; W9A7W4; -.
DR STRING; 171693.BN988_00336; -.
DR eggNOG; COG0768; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000028863; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028863};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..298
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 348..667
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 695 AA; 78694 MW; 76BC2175B3D91B0C CRC64;
MGNKKRKKKA QLPFRINILF FVVFLMFSVL IMQLGVVQIL NGEAFQEEID RTIQDTTKIP
VPRGKIYDTN HNVVVDNKPL YSITYTPAKG TQAEDRLEVA EKLATFISMD SEEYIDGITD
RNKQEYVYLQ DIEKAEDRVT AEEQKELSNS DFYKLVLERI PEEDLKGFSK QELEVIAIKK
ELDKAYSLTP QIVKNEDVTA EEYAQVAEHL SELPGINATT DWDREYPYKD TFRDLVGSIT
SQEQGIPAES EDYYMTRGYS RNDRVGKSGL EEYYEESLRG RKEQIQYTTT KSGRVIDSKT
IVEGERGKDL VLTVDMEFQE EVDKIVREEL KAAKSKHPYA NRYMKDAMAV VLNPQTGEIL
AVSGQSYDEE NDKYISNPLK TLYDAHRPGS IVKGATVLAG YESGVISPGQ TFNDQTIKIA
DTPSKSSYSN LGPVNDYAAL RKSSNVYMFY IALKMGGENR YPFPNDSKAA FDTAAWQQIR
NYFQQFGLGV KTGIDYPYES TGYVGDSSYD PGLLMDFAIG QYDTYTTMQM AQYVSTIAND
GYRVSPHFLK EIREPGESDE KLGSVSKSVN TNVLNRIQMD QTLIERVQEG FRQAYQESGG
TAVSYFGDKD YNPAGKTGTA ENEVYEDGNK TDVNNLSLVG YAPFDEPEVA FAVIAPNTGI
VSNQYNINKY IGERILDAYF DLKEERSEDN EEEEN
//
