ID   YFEW_SALTY              Reviewed;         432 AA.
AC   Q8ZN80;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=STM2478;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL21372.1; -; Genomic_DNA.
DR   RefSeq; NP_461413.1; NC_003197.2.
DR   RefSeq; WP_000673300.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZN80; -.
DR   SMR; Q8ZN80; -.
DR   STRING; 99287.STM2478; -.
DR   MEROPS; S12.A03; -.
DR   PaxDb; Q8ZN80; -.
DR   EnsemblBacteria; AAL21372; AAL21372; STM2478.
DR   GeneID; 1254000; -.
DR   KEGG; stm:STM2478; -.
DR   PATRIC; fig|99287.12.peg.2616; -.
DR   HOGENOM; CLU_020027_1_2_6; -.
DR   OMA; AGWAVRY; -.
DR   PhylomeDB; Q8ZN80; -.
DR   BioCyc; SENT99287:STM2478-MON; -.
DR   Proteomes; UP000001014; 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; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Putative D-alanyl-D-alanine carboxypeptidase"
FT                   /id="PRO_0000036259"
FT   TRANSMEM        7..25
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ   SEQUENCE   432 AA;  47697 MW;  34748A6237929E5D CRC64;
     MKFTLVATVL LTFSLSAFAV EYPVLTTASP DQVGFDSQKL HRLDGWIQNQ IDAGYPSINL
     LVIKDNHIVL QKAWGYAKKY DGSTLLAHPI RATTNTMYDL ASNTKMYATN FALQKLVYEG
     KIDVNDLVSK YIPGFKDMPG DKIKGKNKLR 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