ID YFEW_SALG2 Reviewed; 432 AA.
AC B5RCU8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
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=SG2508;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
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}.
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DR EMBL; AM933173; CAR38334.1; -; Genomic_DNA.
DR RefSeq; WP_000673286.1; NC_011274.1.
DR AlphaFoldDB; B5RCU8; -.
DR SMR; B5RCU8; -.
DR MEROPS; S12.A03; -.
DR KEGG; seg:SG2508; -.
DR HOGENOM; CLU_020027_1_2_6; -.
DR Proteomes; UP000008321; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; DD-peptidase/beta-lactamase superfamily; 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 PANTHER; PTHR43283:SF11; BETA-LACTAMASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43283; BETA-LACTAMASE-RELATED; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 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_5000398406"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01034"
SQ SEQUENCE 432 AA; 47839 MW; E7C3719965D81D2E CRC64;
MKFTLVATVL LTFSLSAFAV EYPVLTIASP DQVGFDSQKL HRLDGWIQNQ IDAGYPSINL
LVIKDNHIVL QKAWGYAKKY DGSTLLAHPI RATTNTMYDL ASNTKMYATN FALQKLVYEG
KIDVNDLVSK YIPGFKDMPG DKIKGKDKLR IIDILHHVAG FPADPQYPNK NVAGKLFSQS
KSTTLEMIKK TPLEYQPRSK HIYSDVDYMI LGFIIESITA MPLDRYVETT IYKPLGLKHT
VFNPLMKGFT PPQIAATELH GNTRDGVIHF PNIRTNTLWG QVHDEKAWYS MGGVSGHAGL
FSDTHDMAVL MQVMLNGGGY GNLKLFDDKT VAQFTRRSPE DATFGLGWRV NGNSSMTPTF
GVLASPQTYG HTGWTGTLTS IDPVNHMAIV ILGNRPHSPV ANPKVNPNVF VSGLLPAATY
GWIVDQIYGS LK
//
