YFEW_SALPA
ID YFEW_SALPA Reviewed; 432 AA.
AC Q5PCQ2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=SPA0391;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76402.1; -; Genomic_DNA.
DR RefSeq; WP_000673301.1; NC_006511.1.
DR AlphaFoldDB; Q5PCQ2; -.
DR SMR; Q5PCQ2; -.
DR MEROPS; S12.A03; -.
DR EnsemblBacteria; AAV76402; AAV76402; SPA0391.
DR KEGG; spt:SPA0391; -.
DR HOGENOM; CLU_020027_1_2_6; -.
DR OMA; AGWAVRY; -.
DR Proteomes; UP000008185; 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_1000149444"
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
