ID I1XFI0_METNJ Unreviewed; 724 AA.
AC I1XFI0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 OrderedLocusNames=Q7A_291 {ECO:0000313|EMBL:AFI83149.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI83149.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI83149.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI83149.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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; CP003390; AFI83149.1; -; Genomic_DNA.
DR RefSeq; WP_014705524.1; NC_017857.3.
DR AlphaFoldDB; I1XFI0; -.
DR STRING; 754476.Q7A_291; -.
DR KEGG; mej:Q7A_291; -.
DR PATRIC; fig|754476.3.peg.288; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_6; -.
DR OMA; RCHYCGY; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000009144; Chromosome.
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; 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};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW 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 205..371
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 465..628
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 724 AA; 81225 MW; AFF2DC0F0E7F940F CRC64;
MSCIVEIALA CPLRQTFDYL SDEPVEHWQP GMRAVIPFGS RQLIGIVIAI KPVSEISTDK
LKKIEQQIDK QSFLPVEIMQ LVQWVSRYYH HPIGECFQAA LPKKLRLGDS DEMQTETYWA
LQQIPVNKPG KKQQQILDLL EDYPEGLSEK ALRVQFGNVK SSLTTLAQQN VITAREHVAL
PVPCLELQQT VSLNNEQKQS IEKVLAEKGQ FSSFLLHGIT GSGKTEVYIE ICREFVENQQ
QVLVLIPEIG LTTQFVERFR HSLAANIVVI NSSVSDADRK QAWLLARSGK ADIIIGTRSA
VFTPMLNPGL MIIDEEHDSS YKQQDGLRYH ARNVALMRAK TLNIPIVLGS ATPSLETLYQ
VKLKRYQLLK LTKRAGGATL PNVKLIAANK TADNNGLSSV LINSIKKHLQ QNHQVLLFIN
RRGFAPVLMC HECNWQANCR SCDAKMVVHQ HQNRLFCHHC GLIQTLPKKC PECGHSELKS
YGVGTEKIEQ ALTAIFNDIP VLRIDRDSTQ RVNAFTNMVK QINQGQAAIL VGTQMLAKGH
DFHDVTLVGV VDADQALFSA DFRATEGLAQ LITQVTGRAG RGKKSGEVLI QSEQPEHPFW
KNLLQDGYEA IAENLLKERI QMELPPHGFW AVWRAEAQEA DLAMQLLQQV AELLQQTASP
VMILGPVPAL MEKRAGRYRA QLLMRSADRA SLHQLIDQHI EAVSKLKLAR KGRWSIDIDP
TELI
//