ID A5FZ50_ACICJ Unreviewed; 718 AA.
AC A5FZ50;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Primosomal protein N' {ECO:0000256|HAMAP-Rule:MF_00983};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent helicase PriA {ECO:0000256|HAMAP-Rule:MF_00983};
GN Name=priA {ECO:0000256|HAMAP-Rule:MF_00983};
GN OrderedLocusNames=Acry_1677 {ECO:0000313|EMBL:ABQ30882.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30882.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30882.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30882.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the restart of stalled replication forks.
CC Recognizes and binds the arrested nascent DNA chain at stalled
CC replication forks. It can open the DNA duplex, via its helicase
CC activity, and promote assembly of the primosome and loading of the
CC major replicative helicase DnaB onto DNA. {ECO:0000256|HAMAP-
CC Rule:MF_00983}.
CC -!- SUBUNIT: Component of the primosome. {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; CP000697; ABQ30882.1; -; Genomic_DNA.
DR RefSeq; WP_011942414.1; NC_009484.1.
DR AlphaFoldDB; A5FZ50; -.
DR STRING; 349163.Acry_1677; -.
DR KEGG; acr:Acry_1677; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_4_0_5; -.
DR Proteomes; UP000000245; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
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.
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; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 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}; DNA replication {ECO:0000256|HAMAP-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 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:UP000000245};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 198..364
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 425..437
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 452..468
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 718 AA; 75362 MW; 2F57C2442F934473 CRC64;
MALVSVLLPY AFDAAFTYEA REAPPPPGAV VTVPLGRRIV HGVVWDDAPE PGIAPARLKT
LHAVIATPAL PGPLRRFIDW VAQYTMAPRG EVLALALKTG LLDPPAPRAG WAAGAAPSGR
ITATRQRVLD ALATLDRPTT AELAAAAGTG AAVVRGLADA GLLRPAARDP SVPLPDPDHA
PPALSAAQEE AAAALRASVA ARRFEVTLLE GVTGAGKTEV FCEAIAACLR EGRQALVLVP
EIALSAQFAA RFAARFGAAP ALWHSGLTQA TRRANYHAVA SGAAKLVLGA RSALFLPFAD
PGLIVVDEEH EAAYKQEDGV TYHARDMAVV RGRISGCAVI LASATPSLES AVNAEAGRYR
HITLAARHGG ARLPAIEAID LRAAPPARGR FLSPVLAGAL ETTLEGGGQA MLFLNRRGYA
PLTLCRGCGH RLTCPNCTAW LVEHRRPGHL LCHHCGHAAQ VPAKCPDCAA EQSFVPIGPG
VERIAEEVAE LFPAARTILM ASDAITTAEQ AEAALRAIVA HEIDLVIGTQ MIAKGWHFPD
LVLVGVVDAD LGLGGGDLRA GERGAQLLHQ VAGRAGRGRL PGRVLLQTYA PEHPVMRALI
GNDLAGFRRA EADLRAPGHW PPFGRLAALI VSADEAATAD AAAAALARTQ PRDGVQVLGP
APAPFAMLRG RHRRRLLLRA PRGIAVQPVL RAWLDRARAE GLPRAARIDI DIDPISFL
//
