ID   RECA_NEIMH              Reviewed;         348 AA.
AC   E6MXY4; P49984; P56988;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN   Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
GN   OrderedLocusNames=NMBH4476_0775; ORFNames=NMH_1222;
OS   Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=909420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H44/76;
RX   PubMed=21378179; DOI=10.1128/jb.01331-10;
RA   Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA   van de Beek D., Pannekoek Y., van der Ende A.;
RT   "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL   J. Bacteriol. 193:2371-2372(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H44/76;
RX   PubMed=21368196; DOI=10.1073/pnas.1019751108;
RA   Budroni S., Siena E., Hotopp J.C., Seib K.L., Serruto D., Nofroni C.,
RA   Comanducci M., Riley D.R., Daugherty S.C., Angiuoli S.V., Covacci A.,
RA   Pizza M., Rappuoli R., Moxon E.R., Tettelin H., Medini D.;
RT   "Neisseria meningitidis is structured in clades associated with restriction
RT   modification systems that modulate homologous recombination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4494-4499(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-297.
RC   STRAIN=H44/76;
RX   PubMed=1406254; DOI=10.1111/j.1365-2958.1992.tb01387.x;
RA   Zhou J., Spratt B.G.;
RT   "Sequence diversity within the argF, fbp and recA genes of natural isolates
RT   of Neisseria meningitidis: interspecies recombination within the argF
RT   gene.";
RL   Mol. Microbiol. 6:2135-2146(1992).
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:0000255|HAMAP-Rule:MF_00268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
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DR   EMBL; AEQZ01000029; EFV63540.1; -; Genomic_DNA.
DR   EMBL; CP002420; ADY95394.1; -; Genomic_DNA.
DR   EMBL; X64849; CAA46061.1; -; Genomic_DNA.
DR   PIR; S24745; S24745.
DR   RefSeq; WP_002216923.1; NZ_AEQZ01000029.1.
DR   AlphaFoldDB; E6MXY4; -.
DR   SMR; E6MXY4; -.
DR   EnsemblBacteria; EFV63540; EFV63540; NMH_1222.
DR   KEGG; nmh:NMBH4476_0775; -.
DR   PATRIC; fig|909420.3.peg.1065; -.
DR   HOGENOM; CLU_040469_3_2_4; -.
DR   OMA; DYGEQAL; -.
DR   BioCyc; NMEN909420:NMBH4476_RS04340-MON; -.
DR   Proteomes; UP000032707; 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: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; -; 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; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45900; PTHR45900; 1.
DR   Pfam; PF00154; RecA; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54752; SSF54752; 1.
DR   TIGRFAMs; TIGR02012; tigrfam_recA; 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; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Nucleotide-binding; SOS response.
FT   CHAIN           1..348
FT                   /note="Protein RecA"
FT                   /id="PRO_0000411249"
FT   BINDING         66..73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   348 AA;  37641 MW;  48AA2079188D7BAF CRC64;
     MSDDKSKALA AALAQIEKSF GKGAIMKMDG SQQEENLEVI STGSLGLDLA LGVGGLPRGR
     IVEIFGPESS GKTTLCLEAV AQCQKNGGVC AFVDAEHAFD PVYARKLGVK VEELYLSQPD
     TGEQALEICD TLVRSGGIDM VVVDSVAALV PKAEIEGDMG DSHVGLQARL MSQALRKLTG
     HIKKTNTLVV FINQIRMKIG VMFGSPETTT GGNALKFYSS VRLDIRRTGS IKKGEEVLGN
     ETRVKVIKNK VAPPFRQAEF DILYGEGISW EGELIDIGVK NDIINKSGAW YSYNGAKIGQ
     GKDNVRVWLK ENPEIADEID AKIRALNGIE MHITEGTQDE TDGERPEE