ID A0A0J5FVY6_9GAMM Unreviewed; 482 AA.
AC A0A0J5FVY6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:KMJ46097.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:KMJ46097.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:KMJ46097.1};
GN ORFNames=AB204_05585 {ECO:0000313|EMBL:KMJ46097.1};
OS Xenorhabdus khoisanae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=880157 {ECO:0000313|EMBL:KMJ46097.1, ECO:0000313|Proteomes:UP000036277};
RN [1] {ECO:0000313|EMBL:KMJ46097.1, ECO:0000313|Proteomes:UP000036277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCB {ECO:0000313|EMBL:KMJ46097.1,
RC ECO:0000313|Proteomes:UP000036277};
RA Naidoo S., Featherston J., Gray V.M.;
RT "Draft Whole-Genome Sequence of the Entomopathogenic Bacterium Xenorhabdus
RT khoisanae.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:KMJ46097.1}.
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DR EMBL; LFCV01000030; KMJ46097.1; -; Genomic_DNA.
DR RefSeq; WP_047962444.1; NZ_LFCV01000030.1.
DR AlphaFoldDB; A0A0J5FVY6; -.
DR STRING; 880157.AB204_05585; -.
DR PATRIC; fig|880157.4.peg.1168; -.
DR Proteomes; UP000036277; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KMJ46097.1};
KW Hydrolase {ECO:0000313|EMBL:KMJ46097.1};
KW Protease {ECO:0000313|EMBL:KMJ46097.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005261037"
SQ SEQUENCE 482 AA; 52856 MW; 371B89732EF9D8FD CRC64;
MALLKITSRI ACMLSLSLSV FSANASSIEE NTQYLPMGTH VSFIAQKVSS KTPLVDYHGQ
QMALPASTQK IVTALAALLQ LSKDYRFITT LESDASISNG ILEGNLTARF VGDPMLTRSQ
LRNMVETLKK SGIKQINGDL IIDVSIFASH DKAPGWVWND MTQCFSSPPS AAIVDKNCFS
VSLYSSEQPG ELAFVHIPSF YPVKVFSEVK TLAKGSPEAK YCELDVTSGD LNRYTLTGCL
TQRDEPLPLA FAVQNGASYA GAILKNELSI ADIELNGAIR RQSIPQRPEK ILALNQSIPL
HSMLSIMLKK SDNMIADTLF RTLGHRYFNV PGTWRSGSDA VRQILKQKAG IDLGNTVMVD
GSGLSRHNLI KPTTMMEILQ FIAQHDNELD FISMLPKAGY DGTLAYRPGL HEAGLDGKVF
AKTGSLQGVY NLAGFMTAAS GQKIAFVQFI SAYSVSPDNQ RTRRVPLARF ENHLYKSLYL
SH
//