ID   RARA_ECOL6              Reviewed;         447 AA.
AC   P0AAZ5; P45526; P75833;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Replication-associated recombination protein A;
GN   Name=rarA; OrderedLocusNames=c1029;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
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DR   EMBL; AE014075; AAN79501.1; -; Genomic_DNA.
DR   RefSeq; WP_000067755.1; NC_004431.1.
DR   AlphaFoldDB; P0AAZ5; -.
DR   SMR; P0AAZ5; -.
DR   STRING; 199310.c1029; -.
DR   EnsemblBacteria; AAN79501; AAN79501; c1029.
DR   GeneID; 66670834; -.
DR   KEGG; ecc:c1029; -.
DR   eggNOG; COG2256; Bacteria.
DR   HOGENOM; CLU_017985_0_3_6; -.
DR   OMA; RIILSQC; -.
DR   BioCyc; ECOL199310:C1029-MON; -.
DR   Proteomes; UP000001410; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
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.
FT   CHAIN           1..447
FT                   /note="Replication-associated recombination protein A"
FT                   /id="PRO_0000168757"
FT   BINDING         57..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P0AAZ4"
SQ   SEQUENCE   447 AA;  49626 MW;  116ACBE38E4E4A3A CRC64;
     MSNLSLDFSD NTFQPLAARM RPENLAQYIG QQHLLAAGKP LPRAIEAGHL HSMILWGPPG
     TGKTTLAEVI ARYANADVER ISAVTSGVKE IREAIERARQ NRNAGRRTIL FVDEVHRFNK
     SQQDAFLPHI EDGTITFIGA TTENPSFELN SALLSRARVY LLKSLSTEDI EQVLTQAMED
     KTRGYGGQDI VLPDETRRAI AELVNGDARR ALNTLEMMAD MAEVDDSGKR VLKPELLTEI
     AGERSARFDN KGDRFYDLIS ALHKSVRGSA PDAALYWYAR IITAGGDPLY VARRCLAIAS
     EDVGNADPRA MQVAIAAWDC FTRVGPAEGE RAIAQAIVYL ACAPKSNAVY TAFKAALADA
     RERPDYDVPV HLRNAPTKLM KEMGYGQEYR YAHDEANAYA AGEVYFPPEI AQTRYYFPTN
     RGLEGKIGEK LAWLAEQDQN SPIKRYR