ID A0A2P2DZ55_9LEPT Unreviewed; 382 AA.
AC A0A2P2DZ55;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ECO:0000313|EMBL:GBF49900.1};
GN ORFNames=LPTSP4_14200 {ECO:0000313|EMBL:GBF49900.1};
OS Leptospira ryugenii.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1917863 {ECO:0000313|EMBL:GBF49900.1, ECO:0000313|Proteomes:UP000245133};
RN [1] {ECO:0000313|EMBL:GBF49900.1, ECO:0000313|Proteomes:UP000245133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YH101 {ECO:0000313|EMBL:GBF49900.1,
RC ECO:0000313|Proteomes:UP000245133};
RA Nakao R., Masuzawa T.;
RT "Novel Leptospira species isolated from soil and water in Japan.";
RL Submitted (FEB-2018) 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}.
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:GBF49900.1}.
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DR EMBL; BFBB01000003; GBF49900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P2DZ55; -.
DR Proteomes; UP000245133; 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:UP000245133};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW ECO:0000256|RuleBase:RU000526}.
FT DOMAIN 52..211
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 216..289
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ SEQUENCE 382 AA; 41753 MW; 3B301D2D2B368BA6 CRC64;
MELSMKKEKS EKTVDKETDQ RKQAIDAALG QIEKQFGKGS IMRLGSDTRM AELNVVSTGS
LDLDIALGIG GFPTGRIIEI YGPESSGKTT LTLSAIAQCQ KKGGIAAFID AEHALDPSYA
KKLGVNVDDL LVAQPDNGEE ALEICESLVR SNAIDLIVID SVAALVPKAE IEGDMGDSHM
GLQARLMSQA LRKLTGTIAK SNTIVIFINQ IRMKIGVMFG SPETTTGGNA LKFYASIRLD
IRRIETLKEK EEPIGNRVRV KVVKNKCAPP FRQAEFDVMY ANGISRESSL IDLAVKHDLI
AKAGSWYSYK SDKIGQGKEQ VKNYLNEHPE IAFTLENQIR DLNGLPLLEE GAKIQTREVK
SIERDPKSKP VSFSTDEVAV GE
//
