ID G9Z2G3_9ENTR Unreviewed; 477 AA.
AC G9Z2G3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EHM49460.1};
GN ORFNames=HMPREF0880_01633 {ECO:0000313|EMBL:EHM49460.1};
OS Yokenella regensburgei ATCC 43003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Yokenella.
OX NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM49460.1, ECO:0000313|Proteomes:UP000003044};
RN [1] {ECO:0000313|EMBL:EHM49460.1, ECO:0000313|Proteomes:UP000003044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM49460.1,
RC ECO:0000313|Proteomes:UP000003044};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:EHM49460.1}.
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DR EMBL; AGCL01000026; EHM49460.1; -; Genomic_DNA.
DR RefSeq; WP_006818119.1; NZ_JH417873.1.
DR AlphaFoldDB; G9Z2G3; -.
DR STRING; 1002368.HMPREF0880_01633; -.
DR MEROPS; S13.001; -.
DR PATRIC; fig|1002368.3.peg.1496; -.
DR HOGENOM; CLU_017692_1_1_6; -.
DR Proteomes; UP000003044; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
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:EHM49460.1};
KW Hydrolase {ECO:0000313|EMBL:EHM49460.1};
KW Protease {ECO:0000313|EMBL:EHM49460.1}; 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_5003529491"
SQ SEQUENCE 477 AA; 51698 MW; 64D5A4917B7D6743 CRC64;
MRFSRFIIGL TTSIAFSVQA ANVEDYLSQL PAGANLALMV QKVGSPAPQI DYHGQQMALP
ASTQKVITAL AALLQLGPDF RFTTTLESKG NVQGGVLKGD LIARFGGDPT LKRQDLRNMV
ATLKKSGVEK IEGNLLIDTS VFASHDKAPG WPWNDLTQCF SAPPAAAIVD RNCFSISLYS
GQKPGDLAFI RVASYYPVTM FSQVRTLQRG SGEAQYCELD VVPGDLNRYT LTGCLPQRAE
PLPLAFAIQD GAAYAGAILK DELKQAGITY SGTLLRQTQV NDPGTVIASK QSAPLHDLLK
IMLKKSDNMI ADTVFRTIGH ARFGVPGTWR AGSDAVRQIL RQQAGVDFGN TIIADGSGLS
RHNLIAPATM MQVLQYIAQH DNELNFISML PLAGYDGSLQ YRAGLHQAGV DGKVSAKTGS
LQGVYNLAGF ITTASGQRMA FVQYLSGYAV EPADQKNRRI PLVRFESRLY KDIYQNN
//
