ID F1Z2R3_9STRE Unreviewed; 792 AA.
AC F1Z2R3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-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:EGE53969.1};
GN ORFNames=SPB_1142 {ECO:0000313|EMBL:EGE53969.1};
OS Streptococcus parauberis NCFD 2020.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE53969.1, ECO:0000313|Proteomes:UP000003732};
RN [1] {ECO:0000313|EMBL:EGE53969.1, ECO:0000313|Proteomes:UP000003732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE53969.1,
RC ECO:0000313|Proteomes:UP000003732};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (FEB-2011) 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:EGE53969.1}.
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DR EMBL; AEUT02000001; EGE53969.1; -; Genomic_DNA.
DR AlphaFoldDB; F1Z2R3; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_9; -.
DR Proteomes; UP000003732; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 269..435
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 533..687
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 498..510
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 525..541
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 792 AA; 90043 MW; AA57B80C79BA7820 CRC64;
MRVAHIIVDI PLMQTDKPFS YAIPDQLIGL VELGSRVHVP FGKSNRLLQG FIVGFSNLDG
DYKEISDLLD VDPVLNSEQL QLADSLRKTV FSYKITLLKA MLPNLLNSHY DKELQVTENT
SLQERNLIFN HKSSVLMSQL TSDQEALALK AIKNGRIEMT YLAKDKKTIK TVSYYKVNKQ
LLMASEISAR AKKKLQLKDF LLSHSEDGKL SDLRKDYSSD VVKYFVSNHL IDSYEEAVNR
SDAYFEKVES SHFLKLNHQQ ETAVQEITQA IGKDSNPFLI EGITGSGKTE VYLHTIDRVL
KMGKTAIVLV PEISLTPQMT NRFISRFGKL VAIMHSGLSD GEKFDEWKKI KTGQARVVVG
ARSAIFAPLE NIGAIIIDEE HESTYKQESN PRYHARDVAL LRAKFHQAVL VLGSATPSIE
SRARASRGLY HFIELTQRAN PLAKIPEVEV VDFRDYIGKQ SLSNYTPYLL DKIKDRLQKN
EQVVLMLNRR GYSSFIMCRD CGYVDGCPNC DISLTLHMDT KSMNCHYCGF QKEIPRICPN
CQSKSIRYYG TGTQKAYDEL LEAIPEARIL RMDVDTTRKK GSHEKILAQF GNHEADILLG
TQMIAKGLDF PNVTLVGVLN ADTSLNLPDF RSSEKTFQLL TQVAGRAGRA EKPGEVLIQT
YNPNHYAIQM AKNQDYEAFY TYEMGIRQKM AYTPYYFTVG ITLSLKDEQE LVIKSYQVMS
ILKENLSDKI KILGPTPKPV ARTHNLYHYQ IIVKYRFENN LEETLNTILD WTQAKGNKDL
KVIIDQEPQN FM
//
