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Database: UniProt
Entry: H8YYL7_9GAMM
LinkDB: H8YYL7_9GAMM
Original site: H8YYL7_9GAMM 
ID   H8YYL7_9GAMM            Unreviewed;       360 AA.
AC   H8YYL7;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Protein RecA {ECO:0000256|ARBA:ARBA00015553, ECO:0000256|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU000526};
GN   Name=recA {ECO:0000256|HAMAP-Rule:MF_00268};
GN   ORFNames=Thi970DRAFT_01214 {ECO:0000313|EMBL:EIC23543.1};
OS   Thiorhodovibrio frisius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiorhodovibrio.
OX   NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC23543.1, ECO:0000313|Proteomes:UP000002964};
RN   [1] {ECO:0000313|Proteomes:UP000002964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EIC23543.1, ECO:0000313|Proteomes:UP000002964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=970 {ECO:0000313|EMBL:EIC23543.1,
RC   ECO:0000313|Proteomes:UP000002964};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA   Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC       stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC       DNA, and the ATP-dependent hybridization of homologous single-stranded
CC       DNAs. It interacts with LexA causing its activation and leading to its
CC       autocatalytic cleavage. {ECO:0000256|HAMAP-Rule:MF_00268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000256|ARBA:ARBA00009391,
CC       ECO:0000256|HAMAP-Rule:MF_00268, ECO:0000256|RuleBase:RU004527}.
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DR   EMBL; JH603168; EIC23543.1; -; Genomic_DNA.
DR   RefSeq; WP_009147626.1; NZ_JH603168.1.
DR   AlphaFoldDB; H8YYL7; -.
DR   STRING; 631362.Thi970DRAFT_01214; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_3_2_6; -.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000002964; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd00983; RecA; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00268; RecA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013765; DNA_recomb/repair_RecA.
DR   InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049261; RecA-like_C.
DR   InterPro; IPR049428; RecA-like_N.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C_sf.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR02012; tigrfam_recA; 1.
DR   PANTHER; PTHR45900:SF1; MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45900; RECA; 1.
DR   Pfam; PF00154; RecA; 1.
DR   Pfam; PF21096; RecA_C; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54752; RecA protein, C-terminal domain; 1.
DR   PROSITE; PS00321; RECA_1; 1.
DR   PROSITE; PS50162; RECA_2; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00268}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00268};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU004527};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00268}; Reference proteome {ECO:0000313|Proteomes:UP000002964};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW   ECO:0000256|RuleBase:RU000526}.
FT   DOMAIN          36..195
FT                   /note="RecA family profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50162"
FT   DOMAIN          200..273
FT                   /note="RecA family profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50163"
FT   REGION          333..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   360 AA;  38369 MW;  3FE53A8512C21A92 CRC64;
     MDDNRKKALA AALGQIEKQF GKGSVMRMGD AGAIRNIEVV STGSLSLDVA LGIGGLPRGR
     VIEIYGPESS GKTTLTLHAV AEMQKTGGTA AFVDAEHALD PQYAEKLGVN MDELLVSQPD
     TGEQALEITD MLVRSGAVDL VVIDSVAALT PKAEIEGEMG DSHVGLQARL MSQALRKLTA
     NIKRSNAIVI FINQIRMKIG VMFGSPETTT GGNALKFYSS VRLDIRRIGS LKKGEEVIGN
     ETKVKVVKNK VAPPFKQVTF DILYGEGISR EGEIIDLGVA GNIIDKSGAW YSYSGNRIGQ
     GKDNVRNYLK ENPDMAADIE AKIRAQLLPS AEALEAEDSS DAGAELPPAK AEKSAKQAET
//
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