ID I3IHG7_9BACT Unreviewed; 366 AA.
AC I3IHG7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-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=KSU1_B0305 {ECO:0000313|EMBL:GAB61162.1};
OS Candidatus Jettenia caeni.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Jettenia.
OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB61162.1, ECO:0000313|Proteomes:UP000002985};
RN [1] {ECO:0000313|EMBL:GAB61162.1, ECO:0000313|Proteomes:UP000002985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA Furukawa K., Fujii T.;
RT "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT reductase instead of a NirS-type with cytochrome cd1.";
RL FEBS Lett. 586:1658-1663(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB61162.1}.
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DR EMBL; BAFH01000002; GAB61162.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IHG7; -.
DR STRING; 247490.KSU1_B0305; -.
DR eggNOG; COG0468; Bacteria.
DR OrthoDB; 9776733at2; -.
DR Proteomes; UP000002985; 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:UP000002985};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW ECO:0000256|RuleBase:RU000526}.
FT DOMAIN 46..205
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 210..284
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT REGION 337..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ SEQUENCE 366 AA; 39800 MW; 4CD131AA87D6460D CRC64;
MGKYTMVKSE VDKEKRQQAL ERAVSQIEKQ YGKGTIMTLG GDTKIDVPTI PTGALSLDIA
LGVGGIPRGR IVEIFGPESS GKTTLTLHII ANAQKNGGTA AFIDAEHALD PDYAKKLGVD
LDNLMVNQPD TGEQALEIAE LLVRSNAVDI IAIDSVAALV PRAEIEGEMG DSHVGLQARL
MSQALRKLTG CISKSQTTVI FINQIREKIG VMYGGNPETT PGGRALKFYS SVRIDIRRIG
SIKDADVAIG NRVRATIAKN KVAAPFKKAE FDILYNTGIS RSGDIIDLGV EHQIIDKSGT
WFSCGEVRLG QGRENSRQFL EENPQLMEEL ERSILKKLRP EMATEKADEG TSQKNKAEPQ
SRKGEK
//
