ID H2ISW7_RAHAC Unreviewed; 477 AA.
AC H2ISW7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family {ECO:0000313|EMBL:AEX50436.1};
GN OrderedLocusNames=Rahaq2_0502 {ECO:0000313|EMBL:AEX50436.1};
OS Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS NCIMB 13365 / CIP 78.65).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX50436.1, ECO:0000313|Proteomes:UP000009010};
RN [1] {ECO:0000313|EMBL:AEX50436.1, ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX PubMed=22582378; DOI=10.1128/JB.00380-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL J. Bacteriol. 194:3020-3021(2012).
RN [2] {ECO:0000313|Proteomes:UP000009010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA Martinez R., Woyke T.;
RT "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; CP003244; AEX50436.1; -; Genomic_DNA.
DR RefSeq; WP_014333694.1; NZ_JMPO01000135.1.
DR AlphaFoldDB; H2ISW7; -.
DR STRING; 745277.Rahaq2_0502; -.
DR MEROPS; S13.001; -.
DR GeneID; 61510643; -.
DR KEGG; raq:Rahaq2_0502; -.
DR PATRIC; fig|745277.3.peg.477; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_017692_1_1_6; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000009010; Chromosome.
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; 1.
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:AEX50436.1};
KW Hydrolase {ECO:0000313|EMBL:AEX50436.1};
KW Protease {ECO:0000313|EMBL:AEX50436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009010};
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_5003562649"
SQ SEQUENCE 477 AA; 51894 MW; FB611ECC10B0F748 CRC64;
MRFLRIVSGL ACAFVLNTNA AQIENYTEYL PDGTNLAVLV QKIGAPAPAI DYHGTQMALP
ASTMKILTAL AALLQLGPDF RFTTTLETPG SVSDGVLKGD LVARFSGDPT LKRQNIRNMV
AVLKKQGVKE ITGDVVINTS VFASHDKAPG WPWNDITQCF SAPPAAAIVD RNCFSVSLYS
APKPDENAFI RVASYYPVHM FSEVRTLAKG SPDAQYCELD VVPGEYNRYT LTGCLTQRSE
PLPLAFAIQD GASYAGAILK DELLQADIQI DGTLKRQTQP TPAGTVLAQT QSAPLHDLLH
QMLKKSDNMI ADTVFRTMGH QRFGVPGTWR AGSDAVRQIL RQKAGVDLGN SIQVDGSGLS
RHDLLSPATM MQVLQYIAQH DKELDFISML PLAGHDGTLQ YRGGLHEAGV DGKVSAKTGS
LSGVYNLAGF ITTASGQRMA FVQFLSGYAV PPEDQRTRRA PLVRFESRLY RDIYQNN
//
