ID   YFEW_SALA4              Reviewed;         432 AA.
AC   B5F0K5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=SeAg_B2622;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
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; CP001138; ACH50914.1; -; Genomic_DNA.
DR   RefSeq; WP_000673289.1; NC_011149.1.
DR   AlphaFoldDB; B5F0K5; -.
DR   SMR; B5F0K5; -.
DR   MEROPS; S12.A03; -.
DR   EnsemblBacteria; ACH50914; ACH50914; SeAg_B2622.
DR   KEGG; sea:SeAg_B2622; -.
DR   HOGENOM; CLU_020027_1_2_6; -.
DR   OMA; AGWAVRY; -.
DR   Proteomes; UP000008819; 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_1000149440"
FT   TRANSMEM        7..25
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ   SEQUENCE   432 AA;  47695 MW;  DCB141642E745833 CRC64;
     MKFTLVATVL LTFSLSAFAV EYPVLTTASP DQVGFDSQKL HRLDGWIQNQ IDAGYPSINL
     LVIKDNHIVL QKAWGYAKKY DGSTLLAHPI LATTNTMYDL ASNTKMYATN FALQKLVYEG
     KIDVNDLVSK YIPDFKDMPG DKIKGKDKLR IIDILHHVAG FPADPQYPNK NVAGKLFSQS
     KSTTLEMIKK TPLEYQPGSK HIYSDVDYMI LGFIIESITA MPLDRYVETT IYKPLGLKHT
     VFNPLMKGFT PPQIAATELH GNTRDGVIHF PNIRTNTLWG QVHDEKAWYS MGGVSGHAGL
     FSDTHDIAVL MQVMLNGGGY GNVKLFDDKT VAQFTRRSPE DATFGLGWRV NGNASMTPTF
     GVLASPQTYG HTGWTGTLTS IDPVNHMAIV ILGNRPHSPV ANPKVNPNVF VSGLLPAATY
     GWIVDQIYGS LK