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Database: UniProt
Entry: Q2GI27_EHRCR
LinkDB: Q2GI27_EHRCR
Original site: Q2GI27_EHRCR 
ID   Q2GI27_EHRCR            Unreviewed;       372 AA.
AC   Q2GI27;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=ECH_0076 {ECO:0000313|EMBL:ABD45217.1};
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD45217.1, ECO:0000313|Proteomes:UP000008320};
RN   [1] {ECO:0000313|EMBL:ABD45217.1, ECO:0000313|Proteomes:UP000008320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is
CC       required for DNA replication and normal SOS inducibility. RecF binds
CC       preferentially to single-stranded, linear DNA. It also seems to bind
CC       ATP. {ECO:0000256|HAMAP-Rule:MF_00365}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00365}.
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DR   EMBL; CP000236; ABD45217.1; -; Genomic_DNA.
DR   RefSeq; WP_006010758.1; NC_007799.1.
DR   AlphaFoldDB; Q2GI27; -.
DR   STRING; 205920.ECH_0076; -.
DR   KEGG; ech:ECH_0076; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_2_0_5; -.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000008320; Chromosome.
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:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.1050.90; RecF/RecN/SMC, N-terminal domain; 1.
DR   HAMAP; MF_00365; RecF; 1.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001238; DNA-binding_RecF.
DR   InterPro; IPR018078; DNA-binding_RecF_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR   PANTHER; PTHR32182:SF0; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR   Pfam; PF13304; AAA_21; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00618; RECF_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00365};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00365};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00365}; Reference proteome {ECO:0000313|Proteomes:UP000008320};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365}.
FT   DOMAIN          32..342
FT                   /note="ATPase AAA-type core"
FT                   /evidence="ECO:0000259|Pfam:PF13304"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   372 AA;  42925 MW;  2D80982D1F93708B CRC64;
     MSSIEKSYIN NLRLVNFRNY INLELDTSSK SVVLLGKNGA GKTNILEAIS LLSKGTGIRG
     VNTESMQNSL SNSPWSVSYQ MHTQNGIYPI AISRNHNKRA ILISNKNQSY TTLHKITSII
     WLIPQLDHIF LKSQSERLRF FDRIAHIFDT KYAIHIIKYN KAKQERSKLL YNNSIDNFWL
     SSLESIIAEN GINIARIRFN VLQTLQNTLS QNSKSHAFFK AIIKIQSQVF NLLDQENSIE
     LYKEHLKNNR SKDSLSNLVN FGVHNDNFQI FHSEKNLIAN YCSTGEQKIL LLSLILSSVF
     AKQNIGEYPI LLLDDVMSHL DAYHQEKLLE IIRDIKCQVW LTDIDLTQQN FTKHKEYFKF
     FHVANNTATL LQ
//
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