ID Q83F46_COXBU Unreviewed; 480 AA.
AC Q83F46;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Peptidase, M20A family {ECO:0000313|EMBL:AAO89669.1};
GN OrderedLocusNames=CBU_0103 {ECO:0000313|EMBL:AAO89669.1};
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377 {ECO:0000313|EMBL:AAO89669.1, ECO:0000313|Proteomes:UP000002671};
RN [1] {ECO:0000313|EMBL:AAO89669.1, ECO:0000313|Proteomes:UP000002671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I
RC {ECO:0000313|Proteomes:UP000002671};
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., Deboy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN [2] {ECO:0000313|EMBL:AAO89669.1, ECO:0000313|Proteomes:UP000002671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I
RC {ECO:0000313|Proteomes:UP000002671};
RX PubMed=19047403; DOI=10.1128/IAI.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J.III., Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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; AE016828; AAO89669.1; -; Genomic_DNA.
DR RefSeq; NP_819155.1; NC_002971.3.
DR RefSeq; WP_010957383.1; NC_002971.4.
DR AlphaFoldDB; Q83F46; -.
DR STRING; 227377.CBU_0103; -.
DR EnsemblBacteria; AAO89669; AAO89669; CBU_0103.
DR GeneID; 1207975; -.
DR KEGG; cbu:CBU_0103; -.
DR PATRIC; fig|227377.7.peg.105; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_029469_0_0_6; -.
DR OrthoDB; 9761532at2; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05682; M20_dipept_dapE; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000002671}.
FT DOMAIN 211..368
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 480 AA; 52896 MW; 430A0660E1504779 CRC64;
MTTSPFEKNA HEIYQTISTL WDDSIIPELA NYIKIPNKSV LFDADWKAHG YMDEAMTLIV
EWCEKQPIKD MKLEVVELPG RTPLLFIEIP GQTDETVLLY GHMDKQPEMK GWDADLGPWK
PVIKEDKLYG RGGADDGYAA FASLTAIAML QRFQIPHARC IVLIEACEES GSADLPFYLH
QLKNRIGNPN FVICLDSGCG NYEQLWCTTS LRGVIGSELK IEVLKTGLHS GTGSGIIPSP
FLILRQLLNR IEDSQTGTII VDELKVDIPP QYIDQAKKTA DALGSVFFEM YPFLSKVEAV
SSNLPELLLN RTWRPQLSVT GIDGLPSVEN AGNVSIPELT VMLSMRLPPT VDGEKASTAL
KAILEKDPPY NAKISFQSDA KASGWMTPPL SEWLAKANET ASQQFFRKPA AYIGEGGTIP
FMGMLGKMFP KAQFMITGLL GPKSNAHGPN EFLHIPTGKK LTACVASVLA SHYENCSVKS
//
