ID G5R1W2_SALSE Unreviewed; 266 AA.
AC G5R1W2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase PBP-6b {ECO:0000313|EMBL:EHC86577.1};
DE Flags: Fragment;
GN ORFNames=LTSESEN_3341 {ECO:0000313|EMBL:EHC86577.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC86577.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC86577.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC86577.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell
CC wall precursors. {ECO:0000256|ARBA:ARBA00003217}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC86577.1}.
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DR EMBL; AFCU01001090; EHC86577.1; -; Genomic_DNA.
DR AlphaFoldDB; G5R1W2; -.
DR MEROPS; S11.009; -.
DR PATRIC; fig|913082.3.peg.2564; -.
DR Proteomes; UP000005065; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.60.410.10; D-Ala-D-Ala carboxypeptidase, C-terminal domain; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015956; Peniciliin-bd_prot_C_sf.
DR InterPro; IPR012907; Peptidase_S11_C.
DR InterPro; IPR037167; Peptidase_S11_C_sf.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF5; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACD; 1.
DR Pfam; PF07943; PBP5_C; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR SMART; SM00936; PBP5_C; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF69189; Penicillin-binding protein associated domain; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:EHC86577.1};
KW Hydrolase {ECO:0000313|EMBL:EHC86577.1};
KW Protease {ECO:0000313|EMBL:EHC86577.1}.
FT DOMAIN 160..251
FT /note="Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00936"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHC86577.1"
SQ SEQUENCE 266 AA; 29633 MW; C95F4E154FF9BA48 CRC64;
RGLIVDSGND ACVALADYIA GGQPQFVAMM NSYVKKLNLQ DTHFETVHGL DAPGQHSSAY
DLAVLSRAII HGEPEFYHMY SEKSLTWNGI TQQNRNGLLW DKTMHIDGLK TGHTSGAGFN
LIASAVDGQR RLIAVVMGAK SSKGREEQAR KLLQWGQQNF ATVQILHSGK KVGSERIWYG
DKEKIALGTE QDFWMALPKA EIPHIKAKYV LDRKELEAPI AAHQQVGEIE LYDRDKLIAQ
WPLVTLESVG KGGMFSRLSD YFQHKA
//
