RARA_COXBU
ID RARA_COXBU Reviewed; 440 AA.
AC P39918;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Replication-associated recombination protein A;
GN Name=rarA; OrderedLocusNames=CBU_1189;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Oswald W.;
RL Thesis (1994), Justus Liebig University / Frankfurt, Germany.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
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).
CC -!- FUNCTION: DNA-dependent ATPase that plays important roles in cellular
CC responses to stalled DNA replication processes.
CC {ECO:0000250|UniProtKB:P0AAZ4}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO90698.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA53291.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X75627; CAA53291.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE016828; AAO90698.1; ALT_INIT; Genomic_DNA.
DR PIR; S43134; S43134.
DR RefSeq; NP_820184.4; NC_002971.3.
DR RefSeq; WP_010958061.1; NC_002971.4.
DR AlphaFoldDB; P39918; -.
DR SMR; P39918; -.
DR STRING; 227377.CBU_1189; -.
DR EnsemblBacteria; AAO90698; AAO90698; CBU_1189.
DR GeneID; 1209093; -.
DR KEGG; cbu:CBU_1189; -.
DR PATRIC; fig|227377.7.peg.1187; -.
DR eggNOG; COG2256; Bacteria.
DR HOGENOM; CLU_017985_0_3_6; -.
DR OMA; RIILSQC; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; Nucleotide-binding; Reference proteome.
FT CHAIN 1..440
FT /note="Replication-associated recombination protein A"
FT /id="PRO_0000168759"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AAZ4"
FT CONFLICT 94
FT /note="R -> RVERAER (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49135 MW; 1C2A364169E28DF8 CRC64;
MLSNNDFIPL ATRMRPGCLE EFVGQSHLLG KDKPLFRAIE KGKLHSMILW GPPGSGKTTL
AEIIAQKAGA RVESISAVLA GVKDIRDVVE RAERHKGQAT ILFVDEVHGF NKSQQDAFLP
HVEKGTITLI GATTENPSFQ LNNALLSRTR VYVLKQLTEA DLLSILENAL ANEERGLGKK
ALEIPEPLRR RIVQFADGDA RQCLNLLEII ADFALEENGR FVVDDGLIDK VLTEGLRRFD
KRGEAFYDQI SALHKSVRGS DPDASLYWLS RLLDGGCDPF YVARRVVRMA SEDIGNADPR
ALQLALDAWE TFERLGTPEG ELAIAQAVVY CACAAKSNAV YKAFNAASRE VKSTGSLEVP
LYLRNAPTRL MKSLDYGKDY RYAHDESDGF AAGVDYLPES LIGRRYYFPI NRGLEIKIKE
KLEYYRKLNE QHKTTEDSKN