ID I7J0I6_9LACO Unreviewed; 797 AA.
AC I7J0I6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=BN53_06550 {ECO:0000313|EMBL:CCI85742.1};
OS Lactobacillus pasteurii DSM 23907 = CRBIP 24.76.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423790 {ECO:0000313|EMBL:CCI85742.1, ECO:0000313|Proteomes:UP000009311};
RN [1] {ECO:0000313|EMBL:CCI85742.1, ECO:0000313|Proteomes:UP000009311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.76T {ECO:0000313|Proteomes:UP000009311};
RA Cousin S., Bouchier C., Loux V., Ma L., Creno S., Bizet C., Clermont D.;
RT "Draft Genome Sequence of Lactobacillus pasteurii CRBIP 24.76T.";
RL Submitted (JUN-2012) 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:CCI85742.1}.
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DR EMBL; CAKD01000023; CCI85742.1; -; Genomic_DNA.
DR RefSeq; WP_009560298.1; NZ_CAKD01000023.1.
DR AlphaFoldDB; I7J0I6; -.
DR STRING; 1423790.BN53_06550; -.
DR PATRIC; fig|1423790.3.peg.94; -.
DR eggNOG; COG1198; Bacteria.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000009311; 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 Reference proteome {ECO:0000313|Proteomes:UP000009311};
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 538..692
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 503..515
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 530..546
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 797 AA; 91019 MW; B71A40AD29210FCD CRC64;
MIAQVIVDIA AKQTDRIFEY HVPDELADIE IGSRVYVPFG PRKLQGFVVG LTDSSEYKGE
LKDLLLVVDE MPPLTKELVQ LSDDLSKDIF SYRISILKAM LPSVMRANYH KILQPADEQA
ANLPIFQGDP LDLNQAMDPK LAGQVRKLLA NKQAKVEYII ENRAKSKTEN QYELLVDKDE
YIKIYNTLRQ NAVKQKQLLM DVIENFDQYP KRQKQLEQDA QVNGATLTNA VKRGWLKKNE
VEVYRDPLKD ESNFVAKKIE LNLQQQDALS KISQSILQTE NKTFLLEGIT GSGKTEVYLH
AIARTLDFGK TALMLVPEIS LTPQMVSQVK ARFGQEVAVL HSGLSEGERY DEWRKIRQGK
TKVVVGARSA IFAPLTNIGL IIIDEEHESS YKQETEPRYH ARDVAIWRSN FNHCPLVLGS
ATPSLASRAR AQKNVYQLLT LTQRANKKQL PQVNLIDLKQ VQFAGSQFDL SVGLVEAIRN
RLEKREQVIL MLNRRGFANF MLCRECGFVL KCPNCDLSLT MHKDSQSMQC HYCGYTTQIP
YRCPNCQSSQ IRFLGTGTQK VQEELLELIP NARILRMDVD TTRRKGSYKK ILDSFANHEA
DILLGTQMIA KGLDFPNVTL VGVVNADTGL WVPDYNSSER TFELLTQVSG RAGRAEKTGE
VLIQTYNPEH YAIKLAQTQD YEQFYRYEMR VRHMGNYPPY FYTVLISIAS KNEQVAAKEA
FKIRRQLQGN LNKDTIILGP TPSAISRLKN QYYYQILVKY KKEDNLNKLL HQIQDDAQGV
KKYGLNIYID KEPERIL
//
