ID Q6KCK4_9LACO Unreviewed; 378 AA.
AC Q6KCK4;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 118.
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:CAF21787.1};
GN ORFNames=EUZ87_09745 {ECO:0000313|EMBL:TBX41156.1}, LPA07_12130
GN {ECO:0000313|EMBL:GEO60892.1};
OS Lactiplantibacillus paraplantarum.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=60520 {ECO:0000313|EMBL:CAF21787.1};
RN [1] {ECO:0000313|EMBL:CAF21787.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain: LMG 16673 {ECO:0000313|EMBL:CAF21787.1};
RX PubMed=16014493; DOI=10.1099/ijs.0.63333-0;
RA Bringel F., Castioni A., Olukoya D.K., Felis G.E., Torriani S.,
RA Dellaglio F.;
RT "Lactobacillus plantarum subsp. argentoratensis subsp. nov., isolated from
RT vegetable matrices.";
RL Int. J. Syst. Evol. Microbiol. 55:1629-1634(2005).
RN [2] {ECO:0000313|EMBL:TBX41156.1, ECO:0000313|Proteomes:UP000292648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSY-TC318 {ECO:0000313|EMBL:TBX41156.1,
RC ECO:0000313|Proteomes:UP000292648};
RA Hussein W.E., Huang E., Yousef A.E.;
RT "Draft genome sequence of Lactobacillus paraplantarum OSY-TC318, a Producer
RT of the novel lantibiotic Paraplantaracin TC318.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEO60892.1, ECO:0000313|Proteomes:UP000321710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 107151 {ECO:0000313|EMBL:GEO60892.1,
RC ECO:0000313|Proteomes:UP000321710};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Lactobacillus paraplantarum NBRC
RT 107151.";
RL Submitted (JUL-2019) 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; AJ621662; CAF21787.1; -; Genomic_DNA.
DR EMBL; BJZG01000014; GEO60892.1; -; Genomic_DNA.
DR EMBL; SEHH01000067; TBX41156.1; -; Genomic_DNA.
DR RefSeq; WP_021732545.1; NZ_RIOB01000007.1.
DR AlphaFoldDB; Q6KCK4; -.
DR GeneID; 79807787; -.
DR Proteomes; UP000292648; Unassembled WGS sequence.
DR Proteomes; UP000321710; 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};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00268}.
FT DOMAIN 35..194
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 199..272
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT REGION 328..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ SEQUENCE 378 AA; 40555 MW; 18510333A07B782E CRC64;
MADARKAALD TALKKIEKNF GKGAIMRMGD AAQTTISTIS SGSLALDDAL GVGGYPRGRI
VEIYGPESSG KTTVALHAVA EVQKQGGTAA YIDAENALDP IYAEHLGVNI DDLLLSQPDT
GEQGLEIADA LVSSGAVDIL VVDSVAALVP RAEIEGEMGD AHVGLQARLM SQALRKLSGT
LNKTKTIALF INQIREKVGV MFGNPETTPG GRALKFYATI RLEVRRAEQI KEGTNIIGNR
VRIKVVKNKV APPFKRAEVD IMYGHGISQT GEIVDMAAEK DIVKKSGSWY SYGDDRIGQG
RENAKKYLDE HPDIMTEIRQ KVRDAYGMDQ TGDEEATETN DQAKDKATAK SASKGQGKTP
KAGPTETALE LDDQPTEK
//
