RECF_STAHJ
ID RECF_STAHJ Reviewed; 371 AA.
AC Q4LAL2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=SH0004;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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. {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; AP006716; BAE03313.1; -; Genomic_DNA.
DR RefSeq; WP_011274362.1; NC_007168.1.
DR AlphaFoldDB; Q4LAL2; -.
DR SMR; Q4LAL2; -.
DR STRING; 279808.SH0004; -.
DR EnsemblBacteria; BAE03313; BAE03313; SH0004.
DR KEGG; sha:SH0004; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_9; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR Proteomes; UP000000543; 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; SOS response.
FT CHAIN 1..371
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196465"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 371 AA; 42648 MW; 4FFD50AEEEC8BDEC CRC64;
MKLKTLQLEN YRNYEEVTLE CHPDVNILIG ENAQGKTNLL ESIYTLALAK SHRTSNDKEL
IRFNSEYAKI EGVLNYRHGT MPLTMFITKK GKQVKVNHLE QSRLTQYVGH LNVVLFAPED
LNIVKGSPQI RRRFIDMELG QISAVYLNDL AQYQRILKQK NNYLKQLQLG QKQDTTMLEV
LNQQFAQYAL NVTLRREHFI KELESLAKPI HAGITNERET LSLTYLPSIK LSDMSKGEQT
LWDEVITLLN DNIKREMDRG VCLFGPHRDD LGFNVNDMDA QTYGSQGQQR TTALSIKLAE
IELMNIEVGE YPILLLDDVL SELDDSRQTH LLSTIQHKVQ TFVTTTSVDG IDHEIMNNAK
LYRINQGEII K
