ID E0E4G6_9FIRM Unreviewed; 770 AA.
AC E0E4G6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:EFM64195.1};
GN ORFNames=HMPREF0634_1343 {ECO:0000313|EMBL:EFM64195.1};
OS Peptostreptococcus stomatis DSM 17678.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64195.1, ECO:0000313|Proteomes:UP000003244};
RN [1] {ECO:0000313|EMBL:EFM64195.1, ECO:0000313|Proteomes:UP000003244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64195.1,
RC ECO:0000313|Proteomes:UP000003244};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFM64195.1}.
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DR EMBL; ADGQ01000066; EFM64195.1; -; Genomic_DNA.
DR AlphaFoldDB; E0E4G6; -.
DR STRING; 596315.HMPREF0634_1343; -.
DR eggNOG; COG1198; Bacteria.
DR Proteomes; UP000003244; 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; 1.
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:UP000003244};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 241..407
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 494..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 469..481
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 496..512
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 770 AA; 88875 MW; 1DF5F35AA302A07B CRC64;
MYIDLILRNM SRFADMLFTY KLPSDMEDHI MIGHRVSLPF GRSNKPIEAF VVAKRKSLGP
DDIEADKIKE IFEILDVEPM LSQENIRLIM WIRNRYMCTY MDALNLFYPK GCRLEAKKVE
EDGQVIWTYK DKKNEKKIRL LSLKYDLDQL DQIISEKKYR LGPKQEDIIR FLSLNESVEA
RSLIEILEVS NQTIKSLIDK DLISVKELDY YRRSEAKFTS PVKKIDLNRD QVQIVDKIKK
GFSLDKKKPF LLHGVTGSGK TEVYMELIEY SLNQGLDSIL LVPEIALTPQ MISRVKGRFG
DIVGVFHSGL SEGQKHDVYR EIKNGNIRIT IGTRSALFLP FRSLGLIIID EEHDMSYHSE
MTPKYSTIEV ARYMSLRQNI SLVMGSATPS VADYYRASQD EYTLLELNNR ANERAMPQIE
IVDMKGEVNR GNRSEISRVL EDEIVKTVNA GNQVILFLNR RGYASSVTCR ECGHVIKCKK
CDISLTYHKF KNMGICHYCG HDEELPRVCP ECSSSNIGIL GLGTEKIEEY INKKYPSIKT
LRIDKDTTSK KGQLESILDT FNRQDADVLI GTQILSKGHD FENVTLVGII SADMMLNYPD
FRSFEQTYQL ITQVAGRAGR GQKKGHVILQ TYNVDHFAIR HAVNYDYKSF YHDEIRLRKA
FGYEPFNNMF RLVFSGKNYN IVRDNATKFI ETVKYLLEAQ SIEIKGILGP NECSINKIND
KYRWQVIIKD EVMDVKGIKS MLRYICISKF DQIFDKDISI NIEINPNSFI
//
