ID A0A1L4BTJ8_9GAMM Unreviewed; 462 AA.
AC A0A1L4BTJ8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:API87144.1};
GN ORFNames=F7310_07140 {ECO:0000313|EMBL:API87144.1};
OS Francisella uliginis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=573570 {ECO:0000313|EMBL:API87144.1, ECO:0000313|Proteomes:UP000184222};
RN [1] {ECO:0000313|EMBL:API87144.1, ECO:0000313|Proteomes:UP000184222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX077310 {ECO:0000313|EMBL:API87144.1,
RC ECO:0000313|Proteomes:UP000184222};
RX PubMed=27881415;
RA Challacombe J.F., Petersen J.M., Gallegos-Graves V., Hodge D., Pillai S.,
RA Kuske C.R.;
RT "Whole genome relationships among Francisella bacteria of diverse origin
RT define new species and provide specific regions for detection.";
RL Appl. Environ. Microbiol. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016796; API87144.1; -; Genomic_DNA.
DR RefSeq; WP_072712831.1; NZ_CP016796.1.
DR AlphaFoldDB; A0A1L4BTJ8; -.
DR STRING; 573570.F7310_07140; -.
DR KEGG; frx:F7310_07140; -.
DR OrthoDB; 9802627at2; -.
DR Proteomes; UP000184222; Chromosome.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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:API87144.1};
KW Hydrolase {ECO:0000313|EMBL:API87144.1};
KW Protease {ECO:0000313|EMBL:API87144.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..462
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012792388"
SQ SEQUENCE 462 AA; 51929 MW; 55AB18511FCF037D CRC64;
MTFNNLLKIL ITFTILLSST SYSLNSTEID KSFDKAVKTN QLNSALIGVK IINLNNGKTI
YSKNADKNFI PASNTKLVTG ATALLYLGKN FKYKTKLYYD KSQNHTLNNL YIVFSGDPSF
TTKDLQNLLS SLKTSEINKI NQVYFVNKFF TGRNTSINES QSSAIFAYGA PSSIYNLNEN
SVILKLTPIK QGFNTEQISG EPLQFKNNLF IATKQQLKTC QFNGYNYYET LTLSGCLPKN
NYTFNFAIQH PKSVMQKAIL RELSKLNITT INNIRITSKL PNNTTLLAEH NSAKLDILLK
HMLVVSDNLY AQTILRTIGY YYNNVGSIVS GKNAVFEILQ NKLKLNTDSI QLEDGAGMSG
NDLLTPNFLT SLLYKMSLDK NYKLFKNMLP IYGETGTLKN FKGDKLKDKV FAKTGTQTTA
IALSGYLIKD NNQYAFSILI NSLKESQKSL AHNFERELLE SL
//
