ID   YFEW_SALPK              Reviewed;         432 AA.
AC   B5BB26;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-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=SSPA0365;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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; FM200053; CAR58489.1; -; Genomic_DNA.
DR   RefSeq; WP_000673301.1; NC_011147.1.
DR   AlphaFoldDB; B5BB26; -.
DR   SMR; B5BB26; -.
DR   MEROPS; S12.A03; -.
DR   KEGG; sek:SSPA0365; -.
DR   HOGENOM; CLU_020027_1_2_6; -.
DR   OMA; AGWAVRY; -.
DR   Proteomes; UP000001869; 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_1000149447"
FT   TRANSMEM        7..25
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ   SEQUENCE   432 AA;  47650 MW;  2807A87115896FB2 CRC64;
     MKFTLVATVL LTFSLSAFAV EYPVLTTASP DQVGFDSQKL HRLDGWIQNQ IDAGYPSINL
     LVIKDNHIVL QKAWGYAKKY DGSTLLAHPI RATTNTMYDL ASNTKMYATN FALQKLVYEG
     KIDVNDLVSK YIPGVKDMPG DKIKGKDKLR IIDILHHVAG FPADPQYPNK NVAGKLFSQS
     KSTTLEMIKK TPLEYQPGSK HIYSDVDYMI LGFIIESITA MPLDRYVETT IYKPLGLKHT
     VFNPLMKGFT PPQIAATELH GNTRDGVIHF PNIRTNTLWG QVHDEKAWYS MGGVSGHAGL
     FSDTHDMAVL MQVMLNGGGY GNVKLFDDKT VAQFTRRSPE DATFGLGWRV NGNASMTPTF
     GVLASPQTYG HTGWTGTLTS IDPVNHMAIV ILGNRPHSPV ANPKVNPNVF VSGLLPAATY
     GWIVDQIYGS LK