ID A9IYY0_BART1 Unreviewed; 735 AA.
AC A9IYY0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
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:CAK02449.1};
GN OrderedLocusNames=BT_2473 {ECO:0000313|EMBL:CAK02449.1};
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640 {ECO:0000313|EMBL:CAK02449.1, ECO:0000313|Proteomes:UP000001592};
RN [1] {ECO:0000313|EMBL:CAK02449.1, ECO:0000313|Proteomes:UP000001592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506 {ECO:0000313|Proteomes:UP000001592};
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK02449.1; -; Genomic_DNA.
DR RefSeq; WP_012232490.1; NC_010161.1.
DR AlphaFoldDB; A9IYY0; -.
DR KEGG; btr:BT_2473; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_4_0_5; -.
DR Proteomes; UP000001592; 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 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 216..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 443..455
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 470..486
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 735 AA; 81486 MW; 3C84E543C9F77E9F CRC64;
MNSNMIEEKV VSVLVPLPVA HAYSYKVPSS MEVEIGSFVR VPVMGRELCG FIVDIEEQTK
NGQRTASVAR EKLRFVLHVF DCPPLKAEMI TFLRFVSRYT MTPFGLVARL VLSVPAALEP
EAQMLGLRYC GGDVERLTPA RLRVLELARN EKIWTRTGLA HAAGTSVSVV EGLKALGIFE
EVKVPAPDLV GMPDPDFCPP QLQGAQNEAA KLLREGVLSS QFQVFLLDGV TGSGKTEVYF
EAVAQAFKGG SQVLILLPEI ALTQQFLDRF YARFGAAAAE WHSDLMPRRR ERVWRQVAEG
RVRVVAGARS ALFLPFHALG LIVVDEEHDS AYKQEERIFY HARDMAVARG SFEHFPVILA
SATPSIESQA NVLKGRYQKV HLPSRFKEVA LPQLRVVDMR QGGVQKGRFI SFALEKALKQ
TLEKGEQALL FLNRRGYAPL TLCRVCGHRF HCTDCSSWLV EHRAQGQLKC HHCGYHQPIP
EACPECGTLD HLVACGPGVE RIAEETQGLF PQARSLILST DLKGGIGQLR SELQAIANGD
VDIIIGTQLV AKGHHFPKLS LVGVIDADLG LANGDLRASE RTFQLLSQVT GRAGRVGLES
LGLLQTYQPD HPVIKALLSC QPEEFYTREI AARQYYHLPP YGRLASLIVS AQQRQAAENY
ARALRQAAPR EKNISVMGPA EAPLALVRGR YRFRLLLQGQ RSFDIQGFIR AMLSNSPKMP
SSVRVQIDID PQSFF
//
