RECF_CALS4
ID RECF_CALS4 Reviewed; 364 AA.
AC Q8RDL3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN Name=recF {ECO:0000255|HAMAP-Rule:MF_00365}; OrderedLocusNames=TTE0004;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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:0000255|HAMAP-Rule:MF_00365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00365}.
CC -!- SIMILARITY: Belongs to the RecF family. {ECO:0000255|HAMAP-
CC Rule:MF_00365}.
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DR EMBL; AE008691; AAM23321.1; -; Genomic_DNA.
DR RefSeq; WP_009610502.1; NC_003869.1.
DR PDB; 5Z67; X-ray; 2.20 A; A=1-361.
DR PDB; 5Z68; X-ray; 3.00 A; A/B/C/D=1-361.
DR PDB; 5Z69; X-ray; 2.10 A; A/B=1-361.
DR PDBsum; 5Z67; -.
DR PDBsum; 5Z68; -.
DR PDBsum; 5Z69; -.
DR AlphaFoldDB; Q8RDL3; -.
DR SMR; Q8RDL3; -.
DR STRING; 273068.TTE0004; -.
DR EnsemblBacteria; AAM23321; AAM23321; TTE0004.
DR KEGG; tte:TTE0004; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_9; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR Proteomes; UP000000555; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..364
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196481"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:5Z69"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:5Z67"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 146..170
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 179..215
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:5Z69"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 284..306
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:5Z69"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:5Z69"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:5Z69"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:5Z69"
SQ SEQUENCE 364 AA; 42276 MW; 6B72069EB26072DC CRC64;
MYLKEIFVDN FRNLKKQKLE FCEGVNLIYG LNAQGKSNLL EAIRLLSMGR SFRGSKMSEL
VKFDEEYFYV RGLVRSADFY EKKIEFGYKV NGNKVIKVNG NKLKSTGEIL GHFLTVIFSP
EDIEIIKEGP SRRRKYLDAC ISVIDKNYFF DLLQYNKTLS NRNSLLKKIK EEGKGEDLLE
IFDEKLAEYG ARIIKVRNNY LEKLKNSMSK FLMEISNEKL EIIYLNSAGV KEVHEENLIR
EKLKNRLTKS LTLDLKYLST QVGPHREDFK ILINGYDSRV YSSQGQKRTA ALCLKLSELE
ILEEETGEKP VLLLDDVMSE LDDNRKKYIL KKLEGFQSFI THTSKSDVEG DCCFKIYDGI
VMRE
