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Database: UniProt
Entry: V9V2C5_9PSED
LinkDB: V9V2C5_9PSED
Original site: V9V2C5_9PSED 
ID   V9V2C5_9PSED            Unreviewed;       441 AA.
AC   V9V2C5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
GN   ORFNames=X970_15900 {ECO:0000313|EMBL:AHC88807.1};
OS   Pseudomonas monteilii SB3101.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1435058 {ECO:0000313|EMBL:AHC88807.1, ECO:0000313|Proteomes:UP000018660};
RN   [1] {ECO:0000313|EMBL:AHC88807.1, ECO:0000313|Proteomes:UP000018660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB3101 {ECO:0000313|EMBL:AHC88807.1,
RC   ECO:0000313|Proteomes:UP000018660};
RA   Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D., Nilsen P.H.,
RA   Nielsen J.L.;
RT   "Complete Genomes of Pseudomonas monteilii SB3078 and SB3101, two Benzene,
RT   Toluene and Ethylbenzene Degrading Bacteria used for Bioaugmentation.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent ATPase that plays important roles in cellular
CC       responses to stalled DNA replication processes.
CC       {ECO:0000256|ARBA:ARBA00002393}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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DR   EMBL; CP006979; AHC88807.1; -; Genomic_DNA.
DR   RefSeq; WP_013973284.1; NC_023076.1.
DR   AlphaFoldDB; V9V2C5; -.
DR   GeneID; 58531776; -.
DR   KEGG; pmot:X970_15900; -.
DR   PATRIC; fig|1435058.3.peg.3100; -.
DR   HOGENOM; CLU_017985_0_3_6; -.
DR   Proteomes; UP000018660; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18139; HLD_clamp_RarA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032423; AAA_assoc_2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR021886; MgsA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR   PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16193; AAA_assoc_2; 1.
DR   Pfam; PF12002; MgsA_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          46..163
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   441 AA;  49221 MW;  3DCF2BEBC6B18C30 CRC64;
     MDLFRSEPVA QPLAARLRPS NLDEYVGQEH LLARGKPLRE ALEQGALHSM IFWGPPGVGK
     TTLARLLAQF CDAHFETVSA VLAGVKEIRQ AVEVAKQQAG QYGRRTILFV DEVHRFNKSQ
     QDAFLPYVED GTLLFIGATT ENPSFELNNA LLSRARVYVL KSLDEAALRK LVNRALTEER
     GLGKRNLRVG DDAFKMLMAA ADGDGRRMLN FLENASDLAE DGSEIDVEML QSLLGDSRRR
     FDKGGEAFYD QISALHKSVR GSNPDGALYW FARMLDGGCD PLYIARRVVR MASEDIGNAD
     PRALSLCLAA WDVQERLGSP EGELAVAQAI TYLACAPKSN AVYMGFKTAL REAAEHGSLE
     VPLHLRNAPT KLMKQLGYGD EYRYAHDEPD AYAAGEDYFP EELEPRQYYQ PVPRGLELKI
     GEKLRHLADL DRNSPRQRRK P
//
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