ID I7H4I5_9HELI Unreviewed; 637 AA.
AC I7H4I5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
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:BAM31775.1};
GN ORFNames=HCBAA847_0528 {ECO:0000313|EMBL:BAM31775.1};
OS Helicobacter cinaedi CCUG 18818 = ATCC BAA-847.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537971 {ECO:0000313|EMBL:BAM31775.1, ECO:0000313|Proteomes:UP000006036};
RN [1] {ECO:0000313|EMBL:BAM31775.1, ECO:0000313|Proteomes:UP000006036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-847 {ECO:0000313|EMBL:BAM31775.1,
RC ECO:0000313|Proteomes:UP000006036};
RX PubMed=23012276; DOI=10.1128/JB.01347-12;
RA Miyoshi-Akiyama T., Takeshita N., Ohmagari N., Kirikae T.;
RT "Complete Genome Sequence of Helicobacter cinaedi Type Strain ATCC
RT BAA-847.";
RL J. Bacteriol. 194:5692-5692(2012).
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; AP012492; BAM31775.1; -; Genomic_DNA.
DR RefSeq; WP_015453307.1; NZ_DS990393.1.
DR AlphaFoldDB; I7H4I5; -.
DR KEGG; hcb:HCBAA847_0528; -.
DR PATRIC; fig|1206745.3.peg.557; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_4_1_7; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000006036; Chromosome 1.
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 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; 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; 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; 1.
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|HAMAP-Rule:MF_00983};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_00983};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00983};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00983};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00983}; Primosome {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 126..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 354..366
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 381..397
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 637 AA; 72212 MW; 17C2C1949B6C9036 CRC64;
MYYYLIAPLG LKSPVLTYGS ETQCVKDELC SINVRNKECL GVVLESTPTP TFKCKILEKT
HLRFLPHQKM LAEFIMQYYC VSLSLSYSLF TPFDESLCVA KDKGNEDSKV DIVPQVKLNL
TQNDALHFLQ THTNPLLFGD TGSGKTEIYI HLIAQTLNEN KNALFLMPEI ALTPQIESRL
RAVFGDMVGI WHSKITKAQK KKFLDKLHNG DIRVIAGARS AFFLPVKNLG LVIVDEEHDD
AYKSQSVPHY NTRDLALYLG KQSEMKVVLG SATPSVSSYF YATKQKSLYR LKGQYFGSKK
HIKILSDTNA NSANDTESAL LPTEMIEKIR QKLEKKEQVI VFLPTRAHYK MLVCQTCGSG
VECAFCSVNM SLHLDKNALM CHYCHWSRAI PRACPQCGSE NLNSFRIGTA QVANFLQRVF
ADSKVALFDR DNITTHKRLK DTLKAFNAGE IDILVGTQML SKGHDYHNVN LAVVLGIDYV
LKSADYRCNE RALSLLYQIA GRAGRKYDGE VWIESANGAF LEQFLGDYED FLHFELSSRP
KIYPPFVRLA TLTFMDRSEK KALENLAKVR NLLQEYPLGQ VEIVGDCKAL LERLYDKYRF
VLLVRSASTR ELLGLLHYVR LQAENLCEIE IDPLNII
//
