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Database: UniProt
Entry: A0A1P8WX21_9SPHN
LinkDB: A0A1P8WX21_9SPHN
Original site: A0A1P8WX21_9SPHN 
ID   A0A1P8WX21_9SPHN        Unreviewed;       369 AA.
AC   A0A1P8WX21;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=BWQ93_08895 {ECO:0000313|EMBL:APZ98603.1};
OS   Sphingopyxis sp. QXT-31.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1357916 {ECO:0000313|EMBL:APZ98603.1, ECO:0000313|Proteomes:UP000188055};
RN   [1] {ECO:0000313|EMBL:APZ98603.1, ECO:0000313|Proteomes:UP000188055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QXT-31 {ECO:0000313|EMBL:APZ98603.1,
RC   ECO:0000313|Proteomes:UP000188055};
RA   Liang J.S.;
RT   "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT   presence of MnII.";
RL   Submitted (JAN-2017) 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}.
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DR   EMBL; CP019449; APZ98603.1; -; Genomic_DNA.
DR   RefSeq; WP_077030234.1; NZ_CP019449.1.
DR   AlphaFoldDB; A0A1P8WX21; -.
DR   STRING; 1357916.BWQ93_08895; -.
DR   KEGG; sphq:BWQ93_08895; -.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000188055; 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; 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; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00617; RECF_1; 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:UP000188055};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          3..336
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   369 AA;  38571 MW;  6E79992D30456B68 CRC64;
     MTIARLSLTD FRNHAAAEMG AGPGLLALHG DNGAGKTNIL EAISLLAPGR GLRRAALSDM
     VRDGATGGFA VFAEVTAGED LAPVALGTGI EPAHPGRRIV RINGASAAAT ALGDWLAILW
     LTPAMDRLFV ETAGNRRRFL DRLVLALDPR HAQHGNRYEA ALRARGKLLA DLASADQQWL
     TSLEAQLAEH GAAMDAARQA TLAALSAELA AQPDAPFARP LLTLVDADGA PRETVWIAGE
     LKALFAARRR IDAAAGRATA GPHRDDLSAV HAASGRSAAR CSTGEQKAML LSLVLAHSDC
     VARLRGQRPI LLLDEVAAHL DPLRRAALYA RLAGQGGQAW LTGTEAALFG DMPGPVTRFR
     IAGGRIAAG
//
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