ID Q8ZLS6_SALTY Unreviewed; 477 AA.
AC Q8ZLS6;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AAL22170.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:AAL22170.1};
GN Name=dacB {ECO:0000313|EMBL:AAL22170.1};
GN OrderedLocusNames=STM3300 {ECO:0000313|EMBL:AAL22170.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL22170.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL22170.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; AE006468; AAL22170.1; -; Genomic_DNA.
DR RefSeq; NP_462211.1; NC_003197.2.
DR RefSeq; WP_001212680.1; NC_003197.2.
DR AlphaFoldDB; Q8ZLS6; -.
DR STRING; 99287.STM3300; -.
DR MEROPS; S13.001; -.
DR PaxDb; 99287-STM3300; -.
DR GeneID; 1254823; -.
DR KEGG; stm:STM3300; -.
DR PATRIC; fig|99287.12.peg.3499; -.
DR HOGENOM; CLU_017692_1_1_6; -.
DR OMA; DGTMRKR; -.
DR PhylomeDB; Q8ZLS6; -.
DR BioCyc; SENT99287:STM3300-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR NCBIfam; TIGR00666; PBP4; 1.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 1.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AAL22170.1};
KW Hydrolase {ECO:0000313|EMBL:AAL22170.1};
KW Protease {ECO:0000313|EMBL:AAL22170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..477
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004318705"
SQ SEQUENCE 477 AA; 51957 MW; BEC171257295348B CRC64;
MRFSRFIIGL TTSIAFSVQA ANIDEYIKQL PAGANLALMV QKIGAPAPAI DYHSQQMALP
ASTQKVITAL AALIQLGPDF RFTTTLETKG NVDNGILKGD VIARFGGDPT LKRQDIRNMV
ATLKKSGVTQ IDGNVLIDTS IFASHDKAPG WPWNDLTQCF SAPPAAAIVD RNCFSVSLYS
AQKPNDLAFI RVASYYPVTM FSQVRTLPRG SADAQYCELD VVPGDLNRYT LTGCLPQRAD
PLPLAFAIQD GASYAGAILK QELKEAGITY RGTLLRQTQV NEPGTIVASK QSAPLHDLLK
IMLKKSDNMI ADTVFRMIGH VRFNVPGTWR AGSDAVRQIL RQQAGIDIGN TIIADGSGLS
RHNLIAPATM MQVLQYIAQH DNELNFISML PLAGYDGSLQ YRAGLHQAGV DGKVSAKTGS
LQGVYNLAGF ITTASGQRMA FVQYLSGYAV PPADQRNRRI PLVRFESRLY KDIYQNN
//
