ID A0A5C6RMM8_9BACT Unreviewed; 848 AA.
AC A0A5C6RMM8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 28-JAN-2026, entry version 22.
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 ECO:0000313|EMBL:TXB62622.1};
GN ORFNames=FRY97_13225 {ECO:0000313|EMBL:TXB62622.1};
OS Phaeodactylibacter luteus.
OC Bacteria; Pseudomonadati; Bacteroidota; Saprospiria; Saprospirales;
OC Haliscomenobacteraceae; Phaeodactylibacter.
OX NCBI_TaxID=1564516 {ECO:0000313|EMBL:TXB62622.1, ECO:0000313|Proteomes:UP000321580};
RN [1] {ECO:0000313|EMBL:TXB62622.1, ECO:0000313|Proteomes:UP000321580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42180 {ECO:0000313|EMBL:TXB62622.1,
RC ECO:0000313|Proteomes:UP000321580};
RA Bowman J.P.;
RT "Genome of Phaeodactylibacter luteus.";
RL Submitted (AUG-2019) 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}.
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:TXB62622.1}.
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DR EMBL; VOOR01000027; TXB62622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6RMM8; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000321580; 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; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00983};
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:UP000321580};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 325..491
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 848 AA; 95540 MW; 50669A28C66819F8 CRC64;
MVQAGLLPGC CICTKKRTNT ILMADALLFH TEGATATYVE VILPLALPKP FTYRVPEALV
QEAAFGKRVE VQFGKSKRYS ALIIGLKSEA PAHDTKPIIS VIDEAPIVTK AQIALWRWMA
DYYLCTLGEV MNAALPANLK LASETVVTLS PLFDRDFEGL NDQEYLIAEA LTLQQELSID
DIRGILQRKS VYPLIRAMLD KRVIYLKEDL QEKYKPKTIG CVRLQEPYAS QPNTLNEAFD
KLSRSGRQTE ALMAYLHLSK QLDFVRKQDV YDKAQVDSTV LRAMEKKGIL EIYDREVSRL
GGYEEETVNA QDLSAQQTTA LEGIKQAFAS EKPVLLHGVT GSGKTRVYTE LMQEAIARGE
QVLYLLPEIA LTTQIISRLE KTFGGDIAIY HSRMSNNERV ELWNSALNGR PVLLGARSSL
FLPFQKLGLI IIDEEHDPSF KQYDPAPRYN ARDTALYLGH LHGSRVLLGT ATPSLESYQN
AQKGKYALVQ MRERFGGLKL PGISLVDLKQ EQKERKLQSH FSSVLLSSLR QTLGRGEQAI
LFQNRRGHSP VYRCTTCGWH AECIHCDVSL TYHKFHNNLR CHYCGYQAAL PPACPACGDK
KLALQGFGTE KIEDELKVYL PEARIARMDL DTVKGKHAHA RLINDFEEGR LDILVGTQMV
TKGLDFEKVA LVGVLSADQL LQYPDFRAGE RAFQLMMQVA GRAGRKHRQG EVLIQGFNTS
HPVLQEVLNG DYAGFFAREM MERQEFHYPP YLRLIRITLK HTKPERVNEA ARLYEKWLKK
ALGQWVMGPA LPTVARVRGY YLLDFMIKIP HGAKNLQKVK AIVREATDNL SLAQGLSSVR
VNTDVDPY
//
