ID   YFEW_SALHS              Reviewed;         432 AA.
AC   B4TD53;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Putative D-alanyl-D-alanine carboxypeptidase {ECO:0000255|HAMAP-Rule:MF_01034};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_01034};
DE   AltName: Full=DD-carboxypeptidase {ECO:0000255|HAMAP-Rule:MF_01034};
DE            Short=DD-CPase {ECO:0000255|HAMAP-Rule:MF_01034};
GN   Name=yfeW {ECO:0000255|HAMAP-Rule:MF_01034}; OrderedLocusNames=SeHA_C2737;
OS   Salmonella heidelberg (strain SL476).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL476;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01034};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01034}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01034}.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family. YfeW subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01034}.
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DR   EMBL; CP001120; ACF66260.1; -; Genomic_DNA.
DR   RefSeq; WP_000673299.1; NC_011083.1.
DR   AlphaFoldDB; B4TD53; -.
DR   SMR; B4TD53; -.
DR   MEROPS; S12.A03; -.
DR   KEGG; seh:SeHA_C2737; -.
DR   HOGENOM; CLU_020027_1_2_6; -.
DR   OMA; AGWAVRY; -.
DR   Proteomes; UP000001866; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   HAMAP; MF_01034; S12_YfeW; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR022849; Pept_S12_YfeW/YbbE-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Protease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Putative D-alanyl-D-alanine carboxypeptidase"
FT                   /id="PRO_1000135853"
FT   TRANSMEM        7..25
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ   SEQUENCE   432 AA;  47679 MW;  66DA0A215978779A CRC64;
     MKFTLVATVL LTFSLSAFAV EYPVLTTASP DQVGFDSQKL HRLDGWIQNQ IDAGYPSINL
     LVIKDNHIVL QKAWGYAKKY DGSTLLAHPI RATTNTMYDL ASNTKMYATN FALQKLVYEG
     KIDVNDLVSK YIPGFKDMPG DKIKGKNKLR IIDILHHVAG FPADPQYPNK NVAGKLFSQS
     KSTTLEMIKK TPLEYQPGSK HIYSDVDYMI LGFIIESITA IPLDRYVETT IYKPLGLKHT
     VFNPLMKGFT PPQIAATELH GNTRDGVIHF PNIRTNTLWG QVHDEKAWYS MGGVSGHAGL
     FSDTHDMAVL MQVMLNGGGY GNVKLFDDKT VAQFTRRSPE DATFGLGWRV NGNASMTPTF
     GVLASPQTYG HTGWTGTLTS IDPVNHMAIV ILGNRPHSPV ANPKVNPNVF VSGLLPAATY
     GWIVDQIYGS LK