ID G0ENE4_BRAIP Unreviewed; 661 AA.
AC G0ENE4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 ECO:0000313|EMBL:AEM23104.1};
GN OrderedLocusNames=Bint_2500 {ECO:0000313|EMBL:AEM23104.1};
OS Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM23104.1, ECO:0000313|Proteomes:UP000008522};
RN [1] {ECO:0000313|EMBL:AEM23104.1, ECO:0000313|Proteomes:UP000008522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA Hafstrom T., Jansson D.S., Segerman B.;
RT "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT features in Brachyspira species and phage-mediated horizontal gene
RT transfer.";
RL BMC Genomics 12:395-395(2011).
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; CP002874; AEM23104.1; -; Genomic_DNA.
DR RefSeq; WP_014488909.1; NC_017243.1.
DR AlphaFoldDB; G0ENE4; -.
DR KEGG; bip:Bint_2500; -.
DR PATRIC; fig|1045858.4.peg.2502; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_4_1_12; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000008522; 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 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; 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; PF00271; Helicase_C; 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.
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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 137..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 400..562
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 365..377
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 392..408
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 661 AA; 75199 MW; A0419655F5DBD963 CRC64;
MYVKVVFNLP IDRILTYRKP DEINDSLVGC RVVAPIKGKN NKGIVVEEVE TIDGNYKVYP
IKARIDLEPI CSDKEFKLAK WMSNYYHSSF GEALFAALPV GTPAKKEKKA KPIPAKQKPY
LKLNEEQEAV LKKINESIES NNPKTFLLHG VTGSGKTEVY LQAIKKVVDM GKQAIVILPE
ISLTPQTIKR FAERFEGKIA VLHSKLSPNS KYRYWQMIKK DEIKIVIGAR SAIFSPTPNL
GIIVIDEEHE TSYKAGDTPR YHARQVAFYR KSHENATLLL GSATPSIESF YYASIGKIEL
LSLKKRAASV NMPEVKILDL KKEKRADAFP MITQKLAEEI NRKLEKKEQI ILFLNRKGYA
PVVTCSYCQR VLECPNCSVS LTYHKKKNVV MCHYCGYTQY LDELCDECKI GHFERIGSGT
EKVEEHLNIL FPNAVVERMD QDTVGGTKNY EKIFKRFSDG EIDILVGTQM IAKGLDFPNV
TLVGVLLADM SLHIPDFRSA ERTFNLITQV AGRSGRGEKN GIVYIQTYSP NNYSIECAKN
HDYISFYNKE IENRKAPLNY PPFSRLIRLV IRGIDEKKVE DDANKIADML RMETYNDSDK
IIILGATACA MSKLNKYYRW NILIKTPSHS LLKNFFNKLN TSFTADKGNY IEIDIDPINM
L
//
