ID A0A1I6BD44_9BACI Unreviewed; 585 AA.
AC A0A1I6BD44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=SAMN04488577_1684 {ECO:0000313|EMBL:SFQ78848.1};
OS Bacillus sp. cl95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ78848.1, ECO:0000313|Proteomes:UP000199578};
RN [1] {ECO:0000313|EMBL:SFQ78848.1, ECO:0000313|Proteomes:UP000199578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL95 {ECO:0000313|EMBL:SFQ78848.1,
RC ECO:0000313|Proteomes:UP000199578};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOYF01000002; SFQ78848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6BD44; -.
DR STRING; 1761761.SAMN04488577_1684; -.
DR OrthoDB; 2985542at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199578; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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 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:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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 Cell cycle {ECO:0000313|EMBL:SFQ78848.1};
KW Cell division {ECO:0000313|EMBL:SFQ78848.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000199578}.
FT DOMAIN 59..204
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 261..560
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 585 AA; 65459 MW; 641A3AED9E932CA4 CRC64;
MWRKRALGMV IFCLIGFSLL LARLAEIQLI STESFSKHNV NLLEASVRQR SQEMVIDNGR
GNFLDRNGES LTHTKIPVLI LFPFLSRMEW DVEKVAEITG VHKEDLIDSI KNAKDPFAFG
DPEPVKLTTS QMEKINALRI PGVFAVERKY EKERFLAEQL IGLVRENPKE LLKRYPDKEL
APETLIGVSG MESSFDEFLL PEGKSKLVFH VDGDGAPLFG INVKYVDPAN PFYPVNIRTT
IDRELQDNSE KLVDQYGIKR GGLVLLDIES NSILAMVSKP SVNKNNPFDG AGLTNMMLKQ
QIAGSVFKTV VAAAAIDYNL DDPGRTFDCS RKLNGKPDLK YNHGMLNFED SFARSCNQTF
GQLAKDLKDI DPDILENYAK KLGVIGRVGW EGPVFHTSNF KQLPEEDVGR VFLSDDAKRD
DNFVALSGIG QHEVRVTPLA VANMMATIAR GGKKESVRAS SKIEYKNGTT MIDFDKTIIK
GDSIAPYTAM NLQRLLREVV LNEKGTGRWF KDLPLEVAGK SGTAETGVFV DKKQLHNKWF
AGYFPYQNPK YALVTVNLDV FEDEGGVNPL FADMVKMIAE NDMNK
//
