RECF_MYCPA
ID RECF_MYCPA Reviewed; 385 AA.
AC Q9L7L5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=DNA replication and repair protein RecF;
GN Name=recF; OrderedLocusNames=MAP_0003;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang Q., Kapur V.;
RT "Genomic organization of the Mycobacterium avium subsp. paratuberculosis
RT origin of replication region.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RecF family. {ECO:0000305}.
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DR EMBL; AF222789; AAF33693.1; -; Genomic_DNA.
DR EMBL; AE016958; AAS02320.1; -; Genomic_DNA.
DR RefSeq; WP_003876778.1; NC_002944.2.
DR AlphaFoldDB; Q9L7L5; -.
DR SMR; Q9L7L5; -.
DR STRING; 262316.MAP_0003; -.
DR EnsemblBacteria; AAS02320; AAS02320; MAP_0003.
DR KEGG; mpa:MAP_0003; -.
DR PATRIC; fig|262316.17.peg.4; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_1_1_11; -.
DR OMA; GESWSYA; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.20.1050.90; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00365; RecF; 1.
DR InterPro; IPR001238; DNA-binding_RecF.
DR InterPro; IPR018078; DNA-binding_RecF_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR042174; RecF_2.
DR PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00611; recf; 1.
DR PROSITE; PS00617; RECF_1; 1.
DR PROSITE; PS00618; RECF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..385
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196433"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 175
FT /note="G -> S (in Ref. 1; AAF33693)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="F -> Y (in Ref. 1; AAF33693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 41956 MW; 191DF24FFB7ADF97 CRC64;
MYVRHLGLRD FRSWAHADLE LQPGRTVFIG SNGFGKTNLL EALWYSSTLG SHRVGTDAPL
IRAGADRAVV STIVVNDGRE CAVDLEIAAG RANKARLNRS PVRSTREVLG VLRAVLFAPE
DLALVRGDPS ERRRYLDDLA TLRRPAIAAV RADYDKVLRQ RTALLKSLSG ARHRGDRGAL
DTLDVWDSRL AEYGAQLMAA RIDLVNQLAP EVEKAYQLLA PGSRAASIGY RSSLGAAASA
EVNAGDRDYL EAALLAGLAA HRDAELERGM CLVGPHRDDL ELWLGEQVAK GFASHGESWS
LALSLRLAAF ELLRADESDP VLLLDDVFAE LDAARRRALA AVAESAEQVL VTAAVLEDIP
TGWQARRLFV ELRDTDAGRV SELRP