ID F5VYA7_9STRE Unreviewed; 798 AA.
AC F5VYA7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:EGL87936.1};
GN ORFNames=HMPREF9967_0665 {ECO:0000313|EMBL:EGL87936.1};
OS Streptococcus infantis SK1076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1005705 {ECO:0000313|EMBL:EGL87936.1, ECO:0000313|Proteomes:UP000010138};
RN [1] {ECO:0000313|EMBL:EGL87936.1, ECO:0000313|Proteomes:UP000010138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1076 {ECO:0000313|EMBL:EGL87936.1,
RC ECO:0000313|Proteomes:UP000010138};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (APR-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:EGL87936.1}.
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DR EMBL; AFNN01000005; EGL87936.1; -; Genomic_DNA.
DR RefSeq; WP_006149887.1; NZ_AFNN01000005.1.
DR AlphaFoldDB; F5VYA7; -.
DR eggNOG; COG1198; Bacteria.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000010138; 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 275..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 539..718
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 504..516
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 531..547
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 798 AA; 90363 MW; 61DF2EEC9440651E CRC64;
MAIAKIIVDV PLMQTDQPYS YKIPEEFKDM LEVGMRVHVP FGKANRLIQG IVLGMEQEND
TEVADEDLKE IAEVLDFSPV LTEEQLWLAE ELRKSVFSYK ISILKAMLPG FLNSSYDKIL
YPLEGLSQED RHRLFGSQDS LAFSSLDLEK QAEMMRLTRK GLLKLEYQAV DQKKVKTQSW
VEVNPDKLEK LEISNRAKKK LELREYLLAH PETVPLADLL EYYSREQVNF FVGRGAVTIV
QKEVQRSAAY FEGIESNQAL ELNPEQKEAC EAVVGAIGKE HPPFLLQGIT GSGKTEVYLQ
IIQGALDMGK TAIVLVPEIS LTPQMTERFI ARFGDKVAIL HSGLSNGEKY DEWRKVERGE
AQVVVGARSA IFAPLKNLGV IIIDEEHEAS YKQDSNPRYH ARDVAILRAQ YNQAALVLGS
ATPSLESRAR AGKGVYQHLR LTQRANPLAS IPEVQVIDFR DYIGQNETSN FTPPLIEAIQ
DRLDKKEQVV LMLNRRGYSS FVMCRECGTV DTCPNCDISL TLHMDTKTMN CHYCGFSKEI
PHVCPNCQSR SIRYYGTGTQ KAYDELAELF PEARILRMDV DTTRKKGSHQ ALLEQFGKGE
ADILLGTQMI AKGLDFPNVT LVGVLNADTA LNLPDFRSSE RTFQLLTQVA GRAGRAEKAG
QVLIQSYNPN HYAIRFAKDQ DYEGFYAYEM GIRRQLGYPP YYFTIGITLS HKKEEEVLRR
AYEVMEILRS GLSDASIILG PTPKPIARTH NLYHYQILIK YRLEDELAST LNQVLALTQE
RENSELRLSI DHEPQQFL
//
