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Database: UniProt
Entry: A0A0Q4MJM3_9GAMM
LinkDB: A0A0Q4MJM3_9GAMM
Original site: A0A0Q4MJM3_9GAMM 
ID   A0A0Q4MJM3_9GAMM        Unreviewed;       447 AA.
AC   A0A0Q4MJM3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Replication-associated recombination protein A {ECO:0000256|ARBA:ARBA00020776};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=ASF13_06925 {ECO:0000313|EMBL:KQN56841.1};
OS   Erwinia sp. Leaf53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN56841.1, ECO:0000313|Proteomes:UP000050856};
RN   [1] {ECO:0000313|EMBL:KQN56841.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56841.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN56841.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN56841.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III
CC       complex. {ECO:0000256|ARBA:ARBA00026073}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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:KQN56841.1}.
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DR   EMBL; LMLK01000021; KQN56841.1; -; Genomic_DNA.
DR   RefSeq; WP_056236905.1; NZ_LMLK01000021.1.
DR   AlphaFoldDB; A0A0Q4MJM3; -.
DR   STRING; 1736225.ASF13_06925; -.
DR   Proteomes; UP000050856; Unassembled WGS sequence.
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:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
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   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          49..165
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   447 AA;  49584 MW;  62BA80BDC7264386 CRC64;
     MSNLSLDFSR NEFQPLAARM RPRTLAEYIG QQHLLAAGKP LPRAIEAGHL HSMILWGPPG
     TGKTTLAEII GHYGQADVER ISAVTSGVKE IREAIERARQ SRNAGRRTIL FVDEVHRFNK
     SQQDAFLPHI EDGTITFIGA TTENPSFELN SALLSRARVY LLKSLTAEDI AVVLDQAMQD
     AERGYGNDNV VLPAKTRDMI AELVNGDARR ALNTLEMMAD MAEVNTAAQR ELTPQLLNEV
     SGERSARFDN KGDRFYDLIS ALHKSVRGSS PDAALYWYAR IITAGGDPLY VARRLLAIAS
     EDVGNADPRG MQVAIAAWDC FTRVGPAEGE RAIAQAIVYL ACAPKSNAVY TAFKAAMRDA
     RDNPDYDVPE HLRNAPTRLM KEMGLGAEYR YAHDEPNAYA AGEDYFPPQM AQTRYYRPVS
     RGLEGKIGEK LAWLAEQDQI SPTKRYR
//
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