ID A0A2T4JW11_9RHOB Unreviewed; 357 AA.
AC A0A2T4JW11;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:PTE22112.1};
GN ORFNames=C5F48_08765 {ECO:0000313|EMBL:PTE22112.1};
OS Cereibacter changlensis JA139.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cereibacter.
OX NCBI_TaxID=1188249 {ECO:0000313|EMBL:PTE22112.1, ECO:0000313|Proteomes:UP000241010};
RN [1] {ECO:0000313|EMBL:PTE22112.1, ECO:0000313|Proteomes:UP000241010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA139 {ECO:0000313|EMBL:PTE22112.1,
RC ECO:0000313|Proteomes:UP000241010};
RA Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA Chintalapati V.R.;
RT "Cereibacter changlensis.";
RL Submitted (MAR-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:PTE22112.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PZKG01000029; PTE22112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4JW11; -.
DR OrthoDB; 9776733at2; -.
DR Proteomes; UP000241010; 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|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00268};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00268};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00268};
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:UP000241010};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW ECO:0000256|RuleBase:RU000526}.
FT DOMAIN 48..207
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 212..285
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT BINDING 78..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ SEQUENCE 357 AA; 38211 MW; 38C5B6B88DBC898E CRC64;
MATANLLDLN GKREMDKAKA LESALAQIER QFGKGSIMKL GANNPVMDVE ATSTGSLGLD
IALGIGGLPK GRIIEIYGPE SSGKTTLTLH VVAEEQKKGG VCAFVDAEHA LDPQYAKKLG
VNLDELLISQ PDTGEQALEI VDTLVRSGAV SLIVVDSVAA LTPKSEIEGE MGDMQMGAQA
RLMSQAMRKL TASIGRSNCM VIFINQIRMK IGVMFGSPET TTGGNALKFY ASVRLDIRRT
GSIKEREDVV GNSTRVKVVK NKVAPPFKQV EFDIMYGEGI SKVGELVDLG VKAGVVEKSG
SWYSYGDERI GQGRENAKTF LKSNPSVAAD IEEKIRASHG LDFSAPEGGK DDEIVDM
//
