YFEW_SALEP
ID YFEW_SALEP Reviewed; 432 AA.
AC B5R4I5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=SEN2457;
OS Salmonella enteritidis PT4 (strain P125109).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P125109;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM933172; CAR34042.1; -; Genomic_DNA.
DR RefSeq; WP_000673284.1; NC_011294.1.
DR AlphaFoldDB; B5R4I5; -.
DR SMR; B5R4I5; -.
DR MEROPS; S12.A03; -.
DR KEGG; set:SEN2457; -.
DR HOGENOM; CLU_020027_1_2_6; -.
DR OMA; AGWAVRY; -.
DR Proteomes; UP000000613; 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_5000397869"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ SEQUENCE 432 AA; 47705 MW; 5DC9D5226062F153 CRC64;
MKFTLVATVL LTFSLSAFAV EYPVLTIASP 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 GNLKLFDDKT VAQFTRHSPE DATFGLGWRV NGNASMTPTF
GVLASPQTYG HTGWTGTLTS IDPVNHMAIV ILGNRPHSPV ANPKVNPNVF VSGLLPAATY
GWIVDQIYGS LK
