ID I4ZSH5_9GAMM Unreviewed; 347 AA.
AC I4ZSH5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:EIM39167.1};
GN ORFNames=HADU_08476 {ECO:0000313|EMBL:EIM39167.1};
OS Acinetobacter sp. HA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM39167.1, ECO:0000313|Proteomes:UP000018434};
RN [1] {ECO:0000313|EMBL:EIM39167.1, ECO:0000313|Proteomes:UP000018434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA {ECO:0000313|EMBL:EIM39167.1,
RC ECO:0000313|Proteomes:UP000018434};
RX PubMed=22933775; DOI=10.1128/JB.01194-12;
RA Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT the Polyphagous Insect Pest Helicoverpa armigera.";
RL J. Bacteriol. 194:5156-5156(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:EIM39167.1}.
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DR EMBL; AJXD01000039; EIM39167.1; -; Genomic_DNA.
DR RefSeq; WP_004812670.1; NZ_AJXD01000039.1.
DR AlphaFoldDB; I4ZSH5; -.
DR PATRIC; fig|1173062.3.peg.1660; -.
DR Proteomes; UP000018434; 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};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00268,
KW ECO:0000256|RuleBase:RU000526}.
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 BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00268"
SQ SEQUENCE 347 AA; 37677 MW; 9E759D7D09EE5AD3 CRC64;
MDENKNKALN AALSQIEKQF GKNTVMRLGD NTVQAVEAVS TGSLTLDIAL GIGGLPKGRI
IEIYGPESSG KTTMTLQAIA ECQKAGGTCA FIDAEHALDP QYARKLGVDI DNLLVSQPDH
GEQALEIADM LVRSGAIDLI VVDSVAALTP RAEIEGEMGD SHMGLQARLM SQALRKITGN
AKRSNCMVIF INQIRMKIGV MFGSPETTTG GNALKFYASV RLDIRRIGQV KEGDEIVGSE
TKVKVVKNKM APPFKEALFQ ILYGKGVNHL GELIDLAVQQ EIVQKAGAWY SYQGDKIGQG
KNNTIRYLEE NKALADTIEK LIREQLLTTG NVVEDKDEEE PADFLDA
//
