ID A0A0C1LB25_9BACT Unreviewed; 833 AA.
AC A0A0C1LB25;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 28-JAN-2026, entry version 44.
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=OI18_21280 {ECO:0000313|EMBL:KIC92728.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia; Chitinophagales;
OC Chitinophagaceae; Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC92728.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC92728.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC92728.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) 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:KIC92728.1}.
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DR EMBL; JSVC01000029; KIC92728.1; -; Genomic_DNA.
DR RefSeq; WP_039143822.1; NZ_JSVC01000029.1.
DR AlphaFoldDB; A0A0C1LB25; -.
DR STRING; 1349421.OI18_21280; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000031408; 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; 3.40.50.300: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.
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:UP000031408};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 309..476
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 559..726
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 539
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 548
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 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 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT BINDING 582
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 833 AA; 94408 MW; 61F3D85619950262 CRC64;
MNKILTETTT DKTASRVVGE NFVEVLIPLA LPKNFTWKVP ARLLPGIKEG IRVEVMLGKS
KKYAGVVKRL HNNKPAAFEP KEVLNVLDDD PIVHPLQLQF WQWMANYYMC SEGEVMQAAL
PTHFKLSSET TVLLNDDAGD DFSSLDDDEF LIAEALTIRK ELKLSEVQQI LSAAHVYPVV
KRLIDKGICL VWEELKHTYK EKKEQFVLLH PAYHQEEKLA DLMNNWSKAP KQLELLLAYL
HLARTSGEVT QSELLKKSGA TAAQLKGLVE KAVLLVEKRS VGRLRQEAAE INISFTLTDA
QQSALEQIKS TFLEKQVCLL HGVTSSGKTL VYVKLIEEML KQGRQVLYML PEIALTAQVI
RRLQQYFGGH IVIYHSRFSQ NERVELWNKV KDGSAKIILG ARSAIFLPYA DLGLIICDEE
HDPSFKQQDP APRYHARDAA IYLGSLFSAK VLLGSATPSL ESFYNAQLGK YGLVQLTSRF
GDLALPEIRF INTKKIVTPD KSRVIISPDL QEAIQQSLGK DKQVILFQNR RGYSPYQVCQ
TCGWIPHCKQ CDVSLTFHKI RNKLVCHYCG TVYPPLTTCE ACGNHHFAQQ NFGTERIEEE
LQEMFPKVRT GRMDVDAIRG KHAHDTLIQL FEQQRIDILV GTQMVVKGLD FEHVSLVGIL
DADAILGFAD FRVYERGFQL MEQVSGRAGR KGEQGKVLIQ VKNTSHPVLQ FVQNHDYIAF
AEAELSNRRQ FAYPPFTRVI QLQFRHRELE KAAAAARQMA DWLKPKFGPY LVGPAAPVVG
RVRNMYLMEL LIKLPKDAQL LQQCKEQIHL LTAHLHHQPP FKSVIVTPDI DPL
//
