ID A0A1M5GHG0_9BACT Unreviewed; 817 AA.
AC A0A1M5GHG0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 10-JUN-2026, entry version 43.
DE RecName: Full=Replication restart protein PriA {ECO:0000256|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent DNA helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_00983};
DE AltName: Full=DNA 3'-5' helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
GN Name=priA {ECO:0000256|HAMAP-Rule:MF_00983};
GN ORFNames=SAMN05444362_1149 {ECO:0000313|EMBL:SHG02941.1};
OS Indolivaga macrotermitis.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Dysgonomonadaceae; Indolivaga.
OX NCBI_TaxID=1346286 {ECO:0000313|EMBL:SHG02941.1, ECO:0000313|Proteomes:UP000184480};
RN [1] {ECO:0000313|Proteomes:UP000184480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27370 {ECO:0000313|Proteomes:UP000184480};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Initiates the restart of stalled replication forks, which
CC reloads the replicative helicase on sites other than the origin of
CC replication. Recognizes and binds to abandoned replication forks and
CC remodels them to uncover a helicase loading site. Promotes assembly of
CC the primosome at these replication forks. {ECO:0000256|HAMAP-
CC Rule:MF_00983}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00048988, ECO:0000256|HAMAP-
CC Rule:MF_00983};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00983};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00983};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00983};
CC -!- SUBUNIT: Component of the replication restart primosome.
CC {ECO:0000256|HAMAP-Rule:MF_00983}.
CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00983}.
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DR EMBL; FQUC01000014; SHG02941.1; -; Genomic_DNA.
DR RefSeq; WP_062181657.1; NZ_BBXL01000014.1.
DR AlphaFoldDB; A0A1M5GHG0; -.
DR STRING; 1346286.SAMN05444362_1149; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000184480; Unassembled WGS sequence.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:TreeGrafter.
DR GO; GO:0006269; P:DNA replication, synthesis of primer; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR CDD; cd17929; DEXHc_priA; 1.
DR CDD; cd18804; SF2_C_priA; 1.
DR FunFam; 3.40.1440.60:FF:000001; Primosomal protein N; 1.
DR FunFam; 3.40.50.300:FF:000489; Primosome assembly protein PriA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.1440.60; PriA, 3(prime) DNA-binding domain; 1.
DR HAMAP; MF_00983; PriA; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR InterPro; IPR041236; PriA_C.
DR InterPro; IPR040498; PriA_CRR.
DR NCBIfam; TIGR00595; priA; 1.
DR PANTHER; PTHR30580; PRIMOSOMAL PROTEIN N; 1.
DR PANTHER; PTHR30580:SF0; PRIMOSOMAL PROTEIN N; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; Zn_ribbon_PriA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00983}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_00983};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00983};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00983};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00983};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00983};
KW Reference proteome {ECO:0000313|Proteomes:UP000184480};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 293..461
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 495..716
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 191..255
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 817 AA; 93405 MW; 45EDE14C998015B3 CRC64;
MLYIDVIVPL PLQGVFTYSV PDSLADQIDI GCRVIVQFGK KKYYTAIIHR IHEDKKLETE
IKEIISVLDK YPIVLPEQLQ FWEWIASYYM CTLGEVSKAA LPAALKLESE THVFLDPEFE
SQVSFTPNEE KIFYILSDTK PLRISEIEKI THISNAIPYV KSLVDKGAAY ISERVKNKYS
AKTETAYRLA KDFSDEELSQ ILDELKRAKK QLQLLYIFLE LRHEAGNPPD FYILKKQLMD
EAAVTAAVLD SLEEKGILNS FRFEVGRFNS IDATLKPIKD LTPDQSKAYN ETNHAFTDKQ
VVLLHGITSS GKTEIYIRLI QDAIDRGEQV LYLLPEISLT AQMTDRLKSV FGNQLMVYHS
KFNDNERAEI WQSLLTKDDC KIVLGARSAI FLPFRKLGLI IVDEEHESSF KQQDPAPRYN
AKNASIVLAA NFGAKVLLGT ATPSIETYYN ALEGRFGLVT LSKRYAEIEL PEVVPVNTKD
LRRRKIMKTI LSPPLLDEMK EALSRKEQVI LFQNRRGFAP LLECKTCSWT PKCEHCDVSL
TYHKGQRVMI CHYCGAVYSV PSQCPECQTP TLDVQGYGTE RIEELVTEQL PEANVVRMDL
DTTRSKRAYE RIIADFELNI TNVLIGTQMV SKGLDFDNVS VVGILNADSM LNYPDFRAHE
RAFQLMTQVS GRAGRKNKRG LVLLQTAHPG HPIISFIRNN DYAGFYETQI NERQLFRYPP
FYRLIEIVLK AKDESLVDSM AGEFGRILRQ TFNDRVLGPV KPTVARIQSL YIRKILLKIE
NQASPSKVRE MIDLCHKYVL QNSKYKSVLL YYDVDPM
//
