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Database: UniProt
Entry: E6K848_9BACT
LinkDB: E6K848_9BACT
Original site: E6K848_9BACT 
ID   E6K848_9BACT            Unreviewed;       372 AA.
AC   E6K848;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|ARBA:ARBA00020170, ECO:0000256|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365,
GN   ECO:0000313|EMBL:EFU30348.1};
GN   ORFNames=HMPREF6485_1627 {ECO:0000313|EMBL:EFU30348.1};
OS   Segatella buccae ATCC 33574.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=873513 {ECO:0000313|EMBL:EFU30348.1, ECO:0000313|Proteomes:UP000003112};
RN   [1] {ECO:0000313|EMBL:EFU30348.1, ECO:0000313|Proteomes:UP000003112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33574 {ECO:0000313|EMBL:EFU30348.1,
RC   ECO:0000313|Proteomes:UP000003112};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (OCT-2010) 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 binds
CC       preferentially to single-stranded, linear DNA. It also seems to bind
CC       ATP. {ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|ARBA:ARBA00008016,
CC       ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578}.
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:EFU30348.1}.
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DR   EMBL; AEPD01000028; EFU30348.1; -; Genomic_DNA.
DR   RefSeq; WP_004345707.1; NZ_GL586311.1.
DR   AlphaFoldDB; E6K848; -.
DR   STRING; 873513.HMPREF6485_1627; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_10; -.
DR   Proteomes; UP000003112; 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: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; IPR003593; AAA+_ATPase.
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   NCBIfam; TIGR00611; recf; 1.
DR   PANTHER; PTHR32182; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR   PANTHER; PTHR32182:SF0; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SMART; SM00382; AAA; 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   ECO:0000256|RuleBase:RU000578};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
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:UP000003112};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          22..363
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   372 AA;  42727 MW;  3277B8F350F8C41B CRC64;
     MVLRKLSIVN YKNIRVTNVD LSPKMNCLIG HNGVGKTNFL DAVYYLSFCR SAFNPVDSQL
     ITHGEDFFVL EGEYDTGAED SEQIYCGMKR GTKKHFKRNK KEYKRLSQHI GLIPLVFVSP
     SDTSLIEGAS EERRHLLDVV IAQYDRSYME SLAAYNKALQ QRNALLKTED GEPDETLMEI
     WEEEMARNGE LIYEKRNDFV RKLIPVFQDI YQHISQQREI VSLKYVSHCQ RGPLLEVIRR
     DRFKDRAVGY SLHGVHRDDL EMLIDGYQLK KEGSQGQNKT FVLALKLAQF NFLKNTTSGT
     TPLLLLDDIF DKLDAQRVEQ IVKLVSGDNF GQIFITDTNR DHLDKILHSS AMDYKIFAVE
     NGELTERGGA DV
//
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