ID A0A2W7MLE3_9BACI Unreviewed; 803 AA.
AC A0A2W7MLE3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=C7437_1011109 {ECO:0000313|EMBL:PZX07987.1};
OS Psychrobacillus insolitus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1461 {ECO:0000313|EMBL:PZX07987.1, ECO:0000313|Proteomes:UP000248646};
RN [1] {ECO:0000313|EMBL:PZX07987.1, ECO:0000313|Proteomes:UP000248646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5 {ECO:0000313|EMBL:PZX07987.1,
RC ECO:0000313|Proteomes:UP000248646};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) 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:PZX07987.1}.
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DR EMBL; QKZI01000001; PZX07987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7MLE3; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000248646; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000248646};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 280..446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 543..697
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 508..520
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 535..551
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 803 AA; 92036 MW; 86E52743DFADCF6B CRC64;
MIAEVIVDVS TFSVDRPFDY IVPEQFVSIV ERGSRVHVPF GNRKVQGFIT NVKEQSDFDE
SKLKEIHSII DVEPVITEEL LQLSKWLTNK TLCFEIDALQ VMLPAALRAS YKKNIKLIEY
QAVDDQFLSL FGKKESVPYD VVEKAGLLKL MKKYLTNGSV ELETIIKQQA RAKTIVKYKV
SPDQDYIQTQ LAGLKKQAVK QKELIEWLLV QEQTSYTLQE LSALAGATSS TVKALIEKNI
LEKEKKEVYR EINSLEHNEI DHRFQLTKEQ EFALSKVNSA QDNAEHTTFL LHGITGSGKT
EIYLNTIEKA ISKGKQAIML VPEISLTPQM TRRFKLRFGE EVAVMHSGLS IGEKYDEWRK
IWRGEVKVVV GARSAIFAPF RDLGVIILDE EHESTYKQED NPRYHARDVA IWRSEFHNCP
VILGSATPSL ESYARSSKGV YTLLTLRMRA KEQPLPTVNV IDMRVELKNG NRSMFSVDLA
DALREKLEKK EQIVLFLNKR GFSSFVLCRD CGTVVECDQC DISLTYHRFN EQLKCHYCGH
EEPVPTICPE CSSEHIRFFG TGTQKVEEEI TKLFPYARVI RMDVDTTRTK GSHERILKQF
GDGEADILLG TQMIAKGLDF PNITLVGVLN ADTTLHLADF RASEKTFQLM TQVSGRAGRH
DKEGEVYIQT YTPEHYAIEL SKSQMYEPFY HKEMQVRKQY EYPPFYYLTL VQVTHENVMI
ASEYAKLATD WLRGNLSSTT MVVGPTACAI SKIQNRYRYQ CLIKYKKEPI LIEKLQQLIK
IYRSDWMKKG IILSIDLDPS AIL
//