RECF_PORG3
ID RECF_PORG3 Reviewed; 364 AA.
AC B2RL41;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=PGN_1567;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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; AP009380; BAG34086.1; -; Genomic_DNA.
DR RefSeq; WP_012458379.1; NZ_CP025930.1.
DR AlphaFoldDB; B2RL41; -.
DR SMR; B2RL41; -.
DR STRING; 431947.PGN_1567; -.
DR EnsemblBacteria; BAG34086; BAG34086; PGN_1567.
DR GeneID; 29256741; -.
DR KEGG; pgn:PGN_1567; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_10; -.
DR OMA; GESWSYA; -.
DR BioCyc; PGIN431947:G1G2V-1767-MON; -.
DR Proteomes; UP000008842; 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; IPR041685; AAA_15.
DR InterPro; IPR001238; DNA-binding_RecF.
DR InterPro; IPR018078; DNA-binding_RecF_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR042174; RecF_2.
DR PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR Pfam; PF13175; AAA_15; 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..364
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000121137"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 364 AA; 41853 MW; 5DBB5294936FB223 CRC64;
MIIEELHIVN FKSIAAADCR FSPKVNCLVG NNGMGKTNLL DALHFLSFCR SHLSVPDNMV
VRHGEEMALL QGLYRDESGD GIELLLSIRP GKHKVLRRNK KEYERLSDHI GHFPLVIVSP
QDYQLILGGS DERRRFMDQQ LCQQDPRYLS ALIQYNRHLQ QRNTMLKQDR HDDALMDVLE
LQMGSYAAEI YNKRSRFIED FLPVFNDLYS DISGSAEKVS LSYRSHLADG IPLEELLRRS
RPKDYLLGFS SCGVHKDELE MLLGGVLIRK IGSEGQNKTF LISMKLAQFR HQQLHGDETP
ILLLDDIFDK LDATRVERII RLVGGNGFGQ IFITDTNRKN LDEIIASWSE DYRLFEIENG
QIFQ