ID A0A1Y6G188_9BACI Unreviewed; 586 AA.
AC A0A1Y6G188;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=SAMN05444673_5166 {ECO:0000313|EMBL:SMQ83057.1};
OS Bacillus sp. OV166.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ83057.1, ECO:0000313|Proteomes:UP000194454};
RN [1] {ECO:0000313|EMBL:SMQ83057.1, ECO:0000313|Proteomes:UP000194454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV166 {ECO:0000313|EMBL:SMQ83057.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FXWM01000001; SMQ83057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6G188; -.
DR OrthoDB; 2985542at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000194454; 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:SMQ83057.1};
KW Cell division {ECO:0000313|EMBL:SMQ83057.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 59..214
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 261..559
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 586 AA; 65821 MW; FB13DE9776836AAB CRC64;
MWRRRAIGWL IISITGLLLL LVRLMHIQLI ETETFSKHNV NLLEESVKQR TQELVIDNGR
GNFLDRNGAM LTHKKVAVLV LFPFLKKMDW ETDKVSSISG IPVTVLKMAV EGAKKPFAYG
DPEPYELTSS QMERINSLKI PGVFAIEKKF ERAQVPAEQL LGMTGENSKE LKKRYPRKEL
SEKTLIGVSG LEESFDEFLL PEGKSKLVYH VDGGGAPLFG INVRYVDPAN PFYPVNIRTT
LDRTLQQKAE NLVDHYQIKK GGLVLLNIQD NSVLSLVSRP TINKNDPYNG AGMTNMMLKQ
QIMGSVFKTV VAAAAIDHNL DDPKRQFDCS KKINGKPELI YNYGMLDFTN SFARSCNRTF
GELASELQKI NPNLLEDYAE KLSLTGSVGW QGDIYHTNDF KQLADEDKGR VFLSEDARKD
ANFAAMSGIG QHEVRATPLA VANMMATIAR GGEKEMVRVV SKIEYKNGTT MVNFPEQSFQ
GDTISPYTAM KLQKLLREVV LNPNGTGRWF KDLPYEVAGK SGTAETGKYE AGRQLHNKWF
AGYFPYENPK YVLVAVNLDV LDTEGGVNLL FADMVKMLYE KDKGMQ
//
