ID W6SHB4_9CLOT Unreviewed; 733 AA.
AC W6SHB4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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:CDM69080.1};
GN ORFNames=CM240_1922 {ECO:0000313|EMBL:CDM69080.1};
OS Clostridium bornimense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM69080.1, ECO:0000313|Proteomes:UP000019426};
RN [1] {ECO:0000313|EMBL:CDM69080.1, ECO:0000313|Proteomes:UP000019426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of Clostridum sp. M2/40.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; HG917868; CDM69080.1; -; Genomic_DNA.
DR RefSeq; WP_044038742.1; NZ_HG917868.1.
DR AlphaFoldDB; W6SHB4; -.
DR STRING; 1216932.CM240_1922; -.
DR KEGG; clt:CM240_1922; -.
DR PATRIC; fig|1216932.3.peg.1921; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_9; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000019426; Chromosome 1.
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.
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:UP000019426};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 212..378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT ZN_FING 440..452
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 467..483
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 733 AA; 84253 MW; 699574633AD43B1B CRC64;
MELYAGIVIE VDHYGLDNIF TYKVPKEMND TIAIGKRVTI PFGVSNKKID GYVYEIYYCR
PESSNGYRIK YIKEIKDDIE HFTEEDKRVI QFIKDKYLAT YIDCIRLITP PGADKGSKIK
IEKKLYIEKP LDGKFAKEPY MSIYNEVQCN EGKYSKSALS KSKSLSLSSI NTLIKHQYIK
EEEKRILRYS SRNYIREEEK NLTLQQSMAL TTINDSFYNK FLIHGVTGSG KTEVFIRLIE
ENLKKDKDVI ILVPEISLTP QMVERIKGRL QIEIGVFHSK MSVGEKYDFW YSIKKKEIKV
AIGPRSALFL PFSNLGLIII DEEHENTYKS ETDPKYDARE VAEFLMDMKG GKVVLASATP
SLESYTKGKN GHYKLIEMED RIPGAVMPKI EVVDMRSELS NGNSSIFSKS LYEKINDRLE
KKEQIILFLN RRGDSSFVSC RACGFVYKCP NCDVSLTLHR SENILECHYC GYRTRPQIKC
PKCKSKYIKF FGIGTEKVER LTKKAFPNAN IERMDLDTMK GRNSFSEVYE RLKNNEIDIL
IGTQMITKGF DFKNVTLVGV LAADLTLNIP QYKSAERTFQ LLTQVAGRAG RGTKEGEVVI
QTYTPGNYAI QRAEKVDYKG FYNDEVDIRQ AMKYPPFGEI LLVNLFYSKE DEVIDTINVL
AKEMKAKFTN LSILGPVPCP ILKINNNFRY QIIIKGELSQ NINKNIKDFV YNIVKKKNSN
IKISVDINPN DLL
//
