ID A0A1I5UB48_9FIRM Unreviewed; 389 AA.
AC A0A1I5UB48;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SFP92521.1};
GN ORFNames=SAMN02910358_00108 {ECO:0000313|EMBL:SFP92521.1};
OS Lachnospiraceae bacterium XBB1006.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520827 {ECO:0000313|EMBL:SFP92521.1, ECO:0000313|Proteomes:UP000199554};
RN [1] {ECO:0000313|EMBL:SFP92521.1, ECO:0000313|Proteomes:UP000199554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBB1006 {ECO:0000313|EMBL:SFP92521.1,
RC ECO:0000313|Proteomes:UP000199554};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; FOXT01000004; SFP92521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5UB48; -.
DR STRING; 1520827.SAMN02910358_00108; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000199554; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 12; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:SFP92521.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:SFP92521.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199554};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..389
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011711031"
FT DOMAIN 29..250
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 62
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 117
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 389 AA; 44817 MW; 354844F4646E2DF1 CRC64;
MKKIICFGLV SMLLFVQIPC HAKPKVQGRQ PTIHAQAACV MDASTYRILW GKNEEKCMPM
ASTTKILTCI LALEKGRLED YVSFSHYATT MPKVHLGAKE GECYRLGDLL YAMMLESYND
VAVAIAEHLA GSVENFQIWM NQKAHRLCGR KLHFVTPNGL DAQGHAITAK NLAKLMAYCT
CFSPKKNEFL AITGCKTHTF KDKSQKRIVC VHNHNRLLGN GFVRSGKTGF TNKAGYCYVA
YMQIHEHPIC VALLADGWPP NSNWKWRDMN ELTRYLEQYG RRERLDFSNI KKPNYFIENQ
KILYSVGDGE LQTTFLYSWE TLRYCIFFQK KKEFPLQKGE RIGEGRAYIN DICIARADLL
CNKTYERITF LKVIKHYFNM FISICIKTR
//
