(data stored in ACNUC7421 zone)

SWISSPROT: D6XUZ8_BACIE

ID   D6XUZ8_BACIE            Unreviewed;       373 AA.
AC   D6XUZ8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   16-JAN-2019, entry version 65.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930555};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=Bsel_0004 {ECO:0000313|EMBL:ADH97556.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97556.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97556.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is
CC       required for DNA replication and normal SOS inducibility. RecF
CC       binds preferentially to single-stranded, linear DNA. It also seems
CC       to bind ATP. {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00032557}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930558}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00365, ECO:0000256|RuleBase:RU000578,
CC       ECO:0000256|SAAS:SAAS00930556}.
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DR   EMBL; CP001791; ADH97556.1; -; Genomic_DNA.
DR   RefSeq; WP_013170986.1; NC_014219.1.
DR   STRING; 439292.Bsel_0004; -.
DR   EnsemblBacteria; ADH97556; ADH97556; Bsel_0004.
DR   KEGG; bse:Bsel_0004; -.
DR   eggNOG; ENOG4105C3X; Bacteria.
DR   eggNOG; COG1195; LUCA.
DR   HOGENOM; HOG000269559; -.
DR   KO; K03629; -.
DR   OMA; GQQKSFL; -.
DR   OrthoDB; 891841at2; -.
DR   BioCyc; BSEL439292:G1GLR-4-MONOMER; -.
DR   Proteomes; UP000000271; 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   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   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;
DR   PRODOM; D6XUZ8.
DR   SWISS-2DPAGE; D6XUZ8.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930557};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|SAAS:SAAS00930531};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354097};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354147};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930553};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930554};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930551};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354122}.
FT   DOMAIN        3    359       SMC_N. {ECO:0000259|Pfam:PF02463}.
FT   NP_BIND      30     37       ATP. {ECO:0000256|HAMAP-Rule:MF_00365}.
SQ   SEQUENCE   373 AA;  43184 MW;  9332202795F0AC77 CRC64;
     MHINELKLTD YRNYTKLHLT FENRVNVFLG ENAQGKTNVM EAIYVLAMAR SHRTAKDREL
     IRWDQPFARV EGAVTNRNGA MKLEMIFSGR GKKVKLNALE RKRLSDYIGA CTIVMFAPED
     LALVKGSPQI RRRFLDMEMG QIFTIYLYYL SQYYKLLKQR NTWLKQLQQK SSSFDEGMWH
     VLTEQLVEAG AEVIQRRFSF LNKLEAWATP IHSAISRDKE TLTLHYESTV KADDEMSVDV
     IKQVFFEQFQ QVMEQEIRRG TTIIGPHRDD VAFFVNDRNV QTYGSQGQQR TAALSVKLAE
     IELIHEKTGE YPILLLDDVL SELDDHRQTH LLNSIQGKVQ TFVTTTSVEG IHHEMLEKAS
     TYLVNDGVIE QQE
//

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