ID A0A099WKD6_9LIST Unreviewed; 800 AA.
AC A0A099WKD6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=EP56_05155 {ECO:0000313|EMBL:KGL44948.1};
OS Listeriaceae bacterium FSL A5-0209.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae.
OX NCBI_TaxID=1497679 {ECO:0000313|EMBL:KGL44948.1, ECO:0000313|Proteomes:UP000029855};
RN [1] {ECO:0000313|EMBL:KGL44948.1, ECO:0000313|Proteomes:UP000029855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0209 {ECO:0000313|EMBL:KGL44948.1,
RC ECO:0000313|Proteomes:UP000029855};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing plants.";
RL Submitted (MAY-2014) 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:KGL44948.1}.
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DR EMBL; JNEZ01000011; KGL44948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099WKD6; -.
DR STRING; 1497679.EP56_05155; -.
DR eggNOG; COG1198; Bacteria.
DR Proteomes; UP000029855; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 278..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 541..698
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 506..518
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 533..549
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 800 AA; 90577 MW; 30C2388C61436106 CRC64;
MARVAQVIVD VPAMQVDRPF DYLIPEAWQD IVRPGMRVSV PFGNRALQGF VVGTSDTSEF
AKLKEIREMM DLAPVLNEEL LELGDWISQE TLAYRITAYQ AMLPAALRAK YEKYFVLLDT
ANDEAQRLFE EYETMDWKRA EQLGALPTLQ KWMKDGIVEL VYQVKNKVTK KTMRVVKPLA
SVQQLEDAMA GLSKGAKAQS KILQFFQVFD EEYISVKALR EKVQTTDATI QKVAALGLIE
IVDQHVSRDP YEHHDFKAST PLPLLPDQQA ARDAIVASAA AGEQETFLLH GVTGSGKTEI
YLQSIEAVLA AGKEAIVLVP EIALTPQMVE RFKRRFGKLV AVLHSALSAG EKYDEWRKIE
QGKAKVVVGA RSAVFAPFLK LGIIIIDEEH ETSYKQEDNP RYHARDVAIE RAKRYGCPVV
LGSATPSLES FARAGKKRYT LLELPTRVND TALPEVEVVD MSEELRNENR TEFSQVLLEK
IKDRLAKKEQ VVLLLNRRGY SSFVMCRDCG YVVECPNCSI SLTYHQAHNQ MKCHYCGYQE
GVPNHCPSCE SEQIRYFGTG TQKVQESLAK LIPEARVIRM DVDTTTKKGS HEKLLNQFRD
KEADVLLGTQ MIAKGLDFPD ITLVGVLNAD TMLNLPDFRA SEKTFQLLTQ VSGRAGRHQL
TGEVIVQSYN PEHYSIQFAK THDYIGFYNH EMRVRKIGSY PPFYYLTLIN VSDEDEMKAV
RTIQEITQFL QGKLGPDAII LGPVPSSIAR IKNKYRYQCI IKYKVEPELK AELKNILLHY
QKEQVKGLTI TMDVQPFVMM
//
