ID A0A0W0R1B3_9GAMM Unreviewed; 721 AA.
AC A0A0W0R1B3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:KTC64837.1};
GN ORFNames=Lade_2131 {ECO:0000313|EMBL:KTC64837.1}, NCTC12735_00225
GN {ECO:0000313|EMBL:VEH82992.1};
OS Legionella adelaidensis.
OG Plasmid 8 {ECO:0000313|EMBL:VEH82992.1, ECO:0000313|Proteomes:UP000281170}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC64837.1, ECO:0000313|Proteomes:UP000054859};
RN [1] {ECO:0000313|EMBL:KTC64837.1, ECO:0000313|Proteomes:UP000054859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC64837.1,
RC ECO:0000313|Proteomes:UP000054859};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Identification of large and diverse effector repertoires of 38 Legionella
RT species.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEH82992.1, ECO:0000313|Proteomes:UP000281170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12735 {ECO:0000313|EMBL:VEH82992.1,
RC ECO:0000313|Proteomes:UP000281170};
RC PLASMID=8 {ECO:0000313|Proteomes:UP000281170};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LNKA01000019; KTC64837.1; -; Genomic_DNA.
DR EMBL; LR134417; VEH82992.1; -; Genomic_DNA.
DR RefSeq; WP_058463254.1; NZ_LR134417.1.
DR AlphaFoldDB; A0A0W0R1B3; -.
DR STRING; 45056.Lade_2131; -.
DR KEGG; ladl:NCTC12735_00225; -.
DR PATRIC; fig|45056.6.peg.2203; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000054859; Unassembled WGS sequence.
DR Proteomes; UP000281170; Plasmid 8.
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 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}; Plasmid {ECO:0000313|EMBL:VEH82992.1};
KW Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00983};
KW Reference proteome {ECO:0000313|Proteomes:UP000054859};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 206..372
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 401..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 430..442
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 457..473
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 721 AA; 81059 MW; 3A6E69DD0D66E843 CRC64;
MPTVLKVCIP NTLRNYFHYF PGEKIPLPGA RVRVPFRNRD KIVGVVIGEE KIEDVKFEIK
QVEEIIDATP LIPLEILNLC SWISTYYQSP LSEVISLALP KKYREGKGVS LPLTKYYSLN
SYPEHAHAQI SSRAKKIHGL IDLLINTKSK EQIQASGFSM LQLKTLIDKN LVRVQEEVNI
PGGYDEPPSL PLPLNEEQNQ AVRAIKNALT SYSCFLLYGV TGSGKTEVYL QVIADVINAG
KQVLILVPEI GLTPQLLSRF TRRFRAPLVV IHSNLNDTER QEAWQLAAFN HAKIIIGTRS
AIFTPLPNLG LIVVDEEHDS SFKQMEGVRY SARDTALIRA YQANIPIILG SATPSLETLY
NSASKYQLFR LTQKALSSTP LHYQIVDTRN QRLEDGLAAI TLKKIGQHLE KGNQVLVFIN
RRGFAPVLLC HSCGWMADCR ACDSHLTLHK KLGKLICHHC GLTQHIIVQC KHCQSQQLFP
LGVGTQRVFE FLKTRFDTSI LRIDRDEIQQ KNALNERLAQ INAGEVKLIV GTQMLAKGHH
FPNLSLVVIL DADNGFYNQD FRGIERLGQL ITQVAGRAGR EKVAGEVVIQ TYLPQHPLLN
TITKEGYPAF ATQLLAMRQA AALPPFSFMA LIRAKAKRQN VVLTFLHTIK EKLMEKNLEI
LGPAPAPLSK KAHFYRMQLM VKSPSRKRLQ AILSELREIV TQEKLNKGIQ WSIDVDPVDL
S
//
