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Database: UniProt
Entry: A0A1C0AC69_9FIRM
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ID   A0A1C0AC69_9FIRM        Unreviewed;       748 AA.
AC   A0A1C0AC69;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   ORFNames=U472_01680 {ECO:0000313|EMBL:OCL27938.1};
OS   Orenia metallireducens.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Orenia.
OX   NCBI_TaxID=1413210 {ECO:0000313|EMBL:OCL27938.1, ECO:0000313|Proteomes:UP000093514};
RN   [1] {ECO:0000313|Proteomes:UP000093514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z6 {ECO:0000313|Proteomes:UP000093514};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OCL27938.1, ECO:0000313|Proteomes:UP000093514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z6 {ECO:0000313|EMBL:OCL27938.1,
RC   ECO:0000313|Proteomes:UP000093514};
RA   Maxim B.I., Kenneth K., Flynn T.M., Oloughlin E.J., Locke R.A., Weber J.R.,
RA   Egan S.M., Mackie R.I., Cann I.K.;
RT   "Orenia metallireducens sp. nov. strain Z6, a Novel Metal-reducing
RT   Firmicute from the Deep Subsurface.";
RL   Submitted (AUG-2016) 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}.
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:OCL27938.1}.
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DR   EMBL; LWDV01000006; OCL27938.1; -; Genomic_DNA.
DR   RefSeq; WP_068714883.1; NZ_LWDV01000006.1.
DR   AlphaFoldDB; A0A1C0AC69; -.
DR   OrthoDB; 9759544at2; -.
DR   Proteomes; UP000093514; Unassembled WGS sequence.
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   CDD; cd17929; DEXHc_priA; 1.
DR   CDD; cd18804; SF2_C_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; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR   Pfam; PF17764; PriA_3primeBD; 1.
DR   Pfam; PF18074; PriA_C; 1.
DR   Pfam; PF18319; PriA_CRR; 1.
DR   Pfam; PF04851; ResIII; 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}; 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:UP000093514};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT   DOMAIN          221..387
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          484..641
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         449..461
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT   ZN_FING         476..492
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   748 AA;  85262 MW;  422A28C7D995B091 CRC64;
     MIKYVEVMVD VSVEQVDRPF TYKVPERLES QIKVGRKVLV PFGRQRVEGY IIREFEADED
     DFEFAVKPIN KVLTDYAFFD EELLKLAKWM SEYYQSYLIS SLKAIVPSGQ TKIKTKQVVK
     LAQSVEESKK LLDKISDRAY KQKEVFSFLI DNPKINLTNT ELAEKLETTS GIIRTLINKG
     YLQYVEKEVK RNPHSHHNFR TTTPLDPTPE QKVAIEEISS ALEQKESSTI LLKGVTGSGK
     TEVYLQVIAK TLESGKDTIV LVPEISLTPQ TIARFKGRFG DQVAVLHSQL SAGERFDEWR
     RIKFGDVKIV VGARSAVFAP FNNLGLIIID EEHETSYKQE DHPKYHAREV AVKRAELVGA
     VTLLGTATPS LEAYHRTEIG EYKLIELKKR IDDRPLPTVE LIDMRKELKT GNKTMFSQPL
     QEGMIDRLKK GEQTMIFLNR RGFSTFVQCR ECGHVMKCND CDVSLTYHAT PNILQCHYCD
     HKEGVPNICP NCESIYIKYF GVGTQKVEEG LKELFPEAKV ARMDVDTTRR KGEYERILSA
     FKQGKIDILV GTQMIAKGHD FSNVTLVGVI TADTALNLPD FRAGERTFQL LTQVAGRTGR
     GEKAGEVIIQ SYTPEHYSIQ FSKNHDYNGF YNFEIETRKF ASYPPFTHII SIVISDERED
     KVIEVSNLLS DIIREKLNKI DDEGIMLLGP VQAPLSRVRG QYRWQLLLKG KELEKIRKVN
     QESLLRLNEL STLKTIKVSV DVDPLGML
//
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