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Database: UniProt
Entry: A0A369Q504_9SPHN
LinkDB: A0A369Q504_9SPHN
Original site: A0A369Q504_9SPHN 
ID   A0A369Q504_9SPHN        Unreviewed;       372 AA.
AC   A0A369Q504;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=HME9302_00700 {ECO:0000313|EMBL:RDC59510.1};
OS   Alteripontixanthobacter maritimus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Alteripontixanthobacter.
OX   NCBI_TaxID=2161824 {ECO:0000313|EMBL:RDC59510.1, ECO:0000313|Proteomes:UP000253727};
RN   [1] {ECO:0000313|EMBL:RDC59510.1, ECO:0000313|Proteomes:UP000253727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HME9302 {ECO:0000313|EMBL:RDC59510.1,
RC   ECO:0000313|Proteomes:UP000253727};
RA   Kang H., Kim H., Joh K.;
RT   "Altererythrobacter sp. HME9302 genome sequencing and assembly.";
RL   Submitted (APR-2018) 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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|ARBA:ARBA00008016,
CC       ECO:0000256|HAMAP-Rule:MF_00365}.
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:RDC59510.1}.
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DR   EMBL; QBKA01000002; RDC59510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369Q504; -.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000253727; 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   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; 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   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365};
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:UP000253727};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365}.
FT   DOMAIN          22..356
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;  39808 MW;  81E7645E2E3B7FF5 CRC64;
     MALTQISLAR FRNHSATTLD DTRRFNLLIG ENGAGKTNVL EAISLLAPGR GLRRAMLPDM
     AEQRGAGGFA VGATLQTDDG GDPVRLGTQT EAAQPTRRLV RINSAAASAL ALGEWLSLSW
     LTPAMDRLFT DSAGARRRFL DRMALALDPA HAGHASRYEA ALRERNRLLS DAQDRGQPAD
     PQWLSAVEPR LAEHGAMLAQ GRARLVGALM EALSALPAEP FARPALTLVP GGPIIREELI
     AALATNRPQD QRAGRTLIGP HRDELEVRMA ASGEADHSAG MEAARCSTGE QKAMLIAITL
     AHAELAARGR PSLLLLDEVA AHLDPVRRTA LFARLREGGA QVWLTGTESA PFADILEEAA
     VWRVGNGVVE RV
//
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