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Database: UniProt
Entry: B3PL40_CELJU
LinkDB: B3PL40_CELJU
Original site: B3PL40_CELJU 
ID   B3PL40_CELJU            Unreviewed;       447 AA.
AC   B3PL40;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
GN   OrderedLocusNames=CJA_2554 {ECO:0000313|EMBL:ACE84341.1};
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84341.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE84341.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84341.1,
RC   ECO:0000313|Proteomes:UP000001036};
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE84341.1; -; Genomic_DNA.
DR   RefSeq; WP_012488150.1; NC_010995.1.
DR   AlphaFoldDB; B3PL40; -.
DR   STRING; 498211.CJA_2554; -.
DR   KEGG; cja:CJA_2554; -.
DR   eggNOG; COG2256; Bacteria.
DR   HOGENOM; CLU_017985_0_3_6; -.
DR   OrthoDB; 9778364at2; -.
DR   Proteomes; UP000001036; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001036}.
FT   DOMAIN          48..165
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   447 AA;  49819 MW;  9F75032DEFB6B914 CRC64;
     MSDLFGNPAP AYQPLAARMR PRNLDDYIGQ EHLLAAGKPL REAITRGQLH SMILWGPPGV
     GKTSLAKLFA EQANARFETL SAVMSGVKEI RAAVAAAEQE RISTRRKTIL FVDEVHRFNK
     SQQDAFLPYV EDGTFIFIGA TTENPSFELN NALLSRCRVY VLRGLQPEQL IQVMRQALTD
     AERGLGKSGL EVDDEVLNSL AQAADGDARK SLNLLEIAAD LAQEQEGVRV INEDVLREVL
     AADVRRFDKG GDIFYEQISA LHKSVRGSSP DGALYWLVRM LDGGCDPLYI ARRVVRMASE
     DIGNADPRAL PLCLSAWDVQ ERLGSPEGEL AIAQAVVYLA CAPKSNAVYN AFNQAMADVR
     TQPAYDVPLH LRNAPTKLMK NMDYGAEYRY AHDEPGAYAA GENYLPEAIA DKRYYHPVER
     GLELKIQEKL AHLRELDQQS RYQRYKK
//
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