YFEW_SALTI
ID YFEW_SALTI Reviewed; 432 AA.
AC Q8Z4S7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN OrderedLocusNames=STY2716, t0381;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07708.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68099.1; -; Genomic_DNA.
DR RefSeq; NP_457012.1; NC_003198.1.
DR RefSeq; WP_000673295.1; NZ_WSUR01000058.1.
DR AlphaFoldDB; Q8Z4S7; -.
DR SMR; Q8Z4S7; -.
DR STRING; 220341.16503694; -.
DR MEROPS; S12.A03; -.
DR EnsemblBacteria; AAO68099; AAO68099; t0381.
DR KEGG; stt:t0381; -.
DR KEGG; sty:STY2716; -.
DR PATRIC; fig|220341.7.peg.2753; -.
DR eggNOG; COG1680; Bacteria.
DR HOGENOM; CLU_020027_1_2_6; -.
DR OMA; AGWAVRY; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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_0000036258"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ SEQUENCE 432 AA; 47697 MW; E7322608F71A36D7 CRC64;
MKFTLVATVL LTFSLSAFAV EYPVLTTASP DQVGFDSQKL HRLDGWIQNQ IDAGYPSINL
LVIKDNHIVL QKAWGYAKKY DGSTLLAHPI RATTNTMYDL ASNTKMYATN FALQKLVYEG
KIDVNDLVSK YIPGFKDMPG DKIKGKDKLR IIDILHHVAG FPADPQYPNK NVAGKLFSQS
KSTTLEMIKK TPLEYQPGSK HIYSDVDYMI LGFIIESITA MPLDRYVETT IYKPLGLKHT
VFNPLMKGFT PPQIAATELH GNTRDGVIHF PNIRTNTLWG QVHDEKAWYS MGGVSGHAGL
FSDTHDMAVL MQVMLNGGGY GNVKLFDNKT VAQFTRRSPE DATFGLGWRV NGNASMTPTF
GVLASPQTYG HTGWTGTLTS IDPVNHMAIV ILGNRPHSPV ANPKVNPNVF VSGLLPAATY
GWIVDQIYGS LK
