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Database: UniProt
Entry: I1XFI0_METNJ
LinkDB: I1XFI0_METNJ
Original site: I1XFI0_METNJ 
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
//
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