ID   RARA_ECOLI              Reviewed;         447 AA.
AC   P0AAZ4; P45526; P75833;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Replication-associated recombination protein A {ECO:0000303|PubMed:11459952};
GN   Name=rarA {ECO:0000303|PubMed:11459952};
GN   Synonyms=mgsA {ECO:0000303|PubMed:15743409}, ycaJ;
GN   OrderedLocusNames=b0892, JW0875;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=7628437; DOI=10.1002/j.1460-2075.1995.tb07342.x;
RA   Matsuyama S., Tajima T., Tokuda H.;
RT   "A novel periplasmic carrier protein involved in the sorting and transport
RT   of Escherichia coli lipoproteins destined for the outer membrane.";
RL   EMBO J. 14:3365-3372(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 367-447.
RC   STRAIN=K12;
RX   PubMed=3029694; DOI=10.1093/nar/15.3.1005;
RA   Haertlein M., Madern D., Leberman R.;
RT   "Cloning and characterization of the gene for Escherichia coli seryl-tRNA
RT   synthetase.";
RL   Nucleic Acids Res. 15:1005-1017(1987).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA   Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT   "Detection of new genes in a bacterial genome using Markov models for three
RT   gene classes.";
RL   Nucleic Acids Res. 23:3554-3562(1995).
RN   [7]
RP   FUNCTION IN RECOMBINATION, DISRUPTION PHENOTYPE, AND GENE NAME.
RX   PubMed=11459952; DOI=10.1073/pnas.111008998;
RA   Barre F.X., Soballe B., Michel B., Aroyo M., Robertson M., Sherratt D.;
RT   "Circles: the replication-recombination-chromosome segregation
RT   connection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8189-8195(2001).
RN   [8]
RP   FUNCTION, AND OVEREXPRESSION.
RX   PubMed=15743409; DOI=10.1111/j.1365-2443.2005.00831.x;
RA   Shibata T., Hishida T., Kubota Y., Han Y.W., Iwasaki H., Shinagawa H.;
RT   "Functional overlap between RecA and MgsA (RarA) in the rescue of stalled
RT   replication forks in Escherichia coli.";
RL   Genes Cells 10:181-191(2005).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, FUNCTION,
RP   ATPASE ACTIVITY, SUBUNIT, INTERACTION WITH SSB, DOMAIN, AND MUTAGENESIS OF
RP   ARG-156.
RX   PubMed=21297161; DOI=10.1074/jbc.m110.210187;
RA   Page A.N., George N.P., Marceau A.H., Cox M.M., Keck J.L.;
RT   "Structure and biochemical activities of Escherichia coli MgsA.";
RL   J. Biol. Chem. 286:12075-12085(2011).
CC   -!- FUNCTION: DNA-dependent ATPase that plays important roles in cellular
CC       responses to stalled DNA replication processes.
CC       {ECO:0000269|PubMed:11459952, ECO:0000269|PubMed:15743409,
CC       ECO:0000269|PubMed:21297161}.
CC   -!- SUBUNIT: Homotetramer. Interacts with the single-stranded DNA-binding
CC       protein (ssb). {ECO:0000269|PubMed:21297161}.
CC   -!- DOMAIN: Contains an N-terminal ATP-binding domain, an adjacent helical
CC       lid domain, and a C-terminal tetramerization domain.
CC       {ECO:0000269|PubMed:21297161}.
CC   -!- DISRUPTION PHENOTYPE: Mutation gives no obvious mutant phenotype, but,
CC       when combined with xer or dif mutants, leads to slower growth.
CC       {ECO:0000269|PubMed:11459952}.
CC   -!- MISCELLANEOUS: Overexpression causes an increase in mutation frequency
CC       and inhibits growth of recA mutant. {ECO:0000269|PubMed:15743409}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=X05017; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00096; AAC73978.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35617.1; -; Genomic_DNA.
DR   EMBL; D49398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X05017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C64828; C64828.
DR   RefSeq; NP_415412.1; NC_000913.3.
DR   RefSeq; WP_000067755.1; NZ_STEB01000006.1.
DR   PDB; 3PVS; X-ray; 2.50 A; A/B/C/D=1-447.
DR   PDBsum; 3PVS; -.
DR   AlphaFoldDB; P0AAZ4; -.
DR   SMR; P0AAZ4; -.
DR   BioGRID; 4259357; 64.
DR   DIP; DIP-48151N; -.
DR   IntAct; P0AAZ4; 7.
DR   STRING; 511145.b0892; -.
DR   jPOST; P0AAZ4; -.
DR   PaxDb; P0AAZ4; -.
DR   PRIDE; P0AAZ4; -.
DR   EnsemblBacteria; AAC73978; AAC73978; b0892.
DR   EnsemblBacteria; BAA35617; BAA35617; BAA35617.
DR   GeneID; 66670834; -.
DR   GeneID; 945505; -.
DR   KEGG; ecj:JW0875; -.
DR   KEGG; eco:b0892; -.
DR   PATRIC; fig|1411691.4.peg.1385; -.
DR   EchoBASE; EB2553; -.
DR   eggNOG; COG2256; Bacteria.
DR   HOGENOM; CLU_017985_0_3_6; -.
DR   InParanoid; P0AAZ4; -.
DR   OMA; RIILSQC; -.
DR   PhylomeDB; P0AAZ4; -.
DR   BioCyc; EcoCyc:EG12690-MON; -.
DR   PRO; PR:P0AAZ4; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030894; C:replisome; IDA:EcoliWiki.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:EcoCyc.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008047; F:enzyme activator activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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:0051289; P:protein homotetramerization; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; DNA replication; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..447
FT                   /note="Replication-associated recombination protein A"
FT                   /id="PRO_0000168755"
FT   BINDING         57..64
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:21297161"
FT   MUTAGEN         156
FT                   /note="R->A: Lack of ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:21297161"
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