ID U2NQQ9_9BACT Unreviewed; 756 AA.
AC U2NQQ9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 28-JAN-2026, entry version 53.
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:ERK40380.1};
GN ORFNames=HMPREF9135_2188 {ECO:0000313|EMBL:ERK40380.1};
OS Segatella baroniae F0067.
OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC Prevotellaceae; Segatella.
OX NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK40380.1, ECO:0000313|Proteomes:UP000016648};
RN [1] {ECO:0000313|EMBL:ERK40380.1, ECO:0000313|Proteomes:UP000016648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0067 {ECO:0000313|EMBL:ERK40380.1,
RC ECO:0000313|Proteomes:UP000016648};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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:ERK40380.1}.
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DR EMBL; AWEY01000006; ERK40380.1; -; Genomic_DNA.
DR RefSeq; WP_021588609.1; NZ_AWEY01000006.1.
DR AlphaFoldDB; U2NQQ9; -.
DR PATRIC; fig|1115809.3.peg.212; -.
DR Proteomes; UP000016648; 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; 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; 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};
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:UP000016648};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 232..400
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 484..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 756 AA; 85797 MW; 9DDE7BCFAE24C11B CRC64;
MSYVDVILPL PLDGLFTYSV PAEKAPRVVP GVRLLVPLGK SKTYTAIAVE LHERQPDFEA
RPILDVLDAA PVLLPQQLKL WQWIADYYLA PLGDVYKAAL PAGLKAEEGF RPRTETYIAL
SESCRNEQTL HACLNMLARA TKQLHAFTTF LSLSRWDTLS GTAPGSPVVE VTREELMNAS
HCTAAVVKAL VDRRFLFTYE KTVGRLNVGG EPRLDSIQPL SLPQQDAYNQ IVFQFLNKPV
VLLHGVTSSG KTEVYIHLIR KALEERKQVL YLLPEIALTV QITTRLQRIF GNRMAVYHSK
YSDAERVEIW NRQLSADPYD VILGARSAVF LPFRNLGLVI VDEEHETSFK QQDPAPRYHA
RSAAIMLARM YGARTLLGTA TPSMESYYNA HQGKYGLVGL MTRYRDIRLP EIRVVDIKDL
QRRKMMNGPF SPDLLQAVRQ ALHDGRQVIL FQNRRGFAPM VECRTCGWVP KCGNCDVSLT
LHKRLNQLTC HYCGFTYTVP TVCPNCGGTE LQGRGYGTEK IEDYIRELFP EARVARMDLD
TTRTRNAYER LIGDFSRGKT NLLIGTQMVS KGLDFDKVSV VGILNADSML NYPDFRAYEH
AFMMMSQVSG RAGRRGDRGL VILQTKSADL PVVRQVVTND YEGFYNELLE ERQLFHYPPF
HHLVYVFLKH KYENVAETAG LELGGRLRQY FGGRVLGPDK PAIARVKALH IRKLVLKLEN
GLNLSQAREA LRYVQKQMMQ DKRYAALQIY YDVDPL
//
