ID H8MTK4_CORCM Unreviewed; 797 AA.
AC H8MTK4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:AFE09982.1};
GN OrderedLocusNames=COCOR_01330 {ECO:0000313|EMBL:AFE09982.1};
OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS (Myxococcus coralloides).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Corallococcus.
OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE09982.1, ECO:0000313|Proteomes:UP000007587};
RN [1] {ECO:0000313|EMBL:AFE09982.1, ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RX PubMed=22582372; DOI=10.1128/JB.00397-12;
RA Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA Sogaard-Andersen L.;
RT "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT coralloides DSM 2259.";
RL J. Bacteriol. 194:3012-3013(2012).
RN [2] {ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT DSM 2259.";
RL Submitted (MAR-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}.
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DR EMBL; CP003389; AFE09982.1; -; Genomic_DNA.
DR AlphaFoldDB; H8MTK4; -.
DR STRING; 1144275.COCOR_01330; -.
DR KEGG; ccx:COCOR_01330; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_7; -.
DR InParanoid; H8MTK4; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000007587; 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 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:UP000007587};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 269..435
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 537..690
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 502..514
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 529..545
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 86779 MW; EB4558E8DBA239DD CRC64;
MEQEHFALGG FPRAQGEAPS RGSIPLRTRR TEVGREVSQR DPAATVRPVV SATPAQLASV
AVGRPVRGEF TYLVPEALAG NLAPGQRVLV PFGRGMALGF YLGPANAPVE GGVRLKPIQR
VLEDSPSLPK DLIALLRFTA EHYRYPLGEV IRGALPPGLS TAVDEKEARP DIQFFVEALV
TEVPPALARA PAQAAVLQYL LAVGGRAPLD EVTHAIPGAR ETLKKLATRK FVKWVEVTLQ
PGVREGLVQN RPDRLTPEQA LAVKELQGAV DVGGFQPYLL HGVTGSGKTE VYLRAVEHTL
ARGLGSLVLV PEIALTPQLV GRFRSRFGGD VAVLHSGLKD RERLFHWQAL RKGTVKIAVG
VRSAVFAPVE HLGLIVVDEE HDPSFKQDEK LRYQARDLAV VRGKQASAVV VLGSATPSLE
TLQNTRSGRY KLIELKNRVD DRPMPTINLV DLRVERPREG QVTEEAPILS PQMLQAMEET
VTKGQQVILF LNRRGHSTIL LCEVCGLSLK CHDCDVCMTH HRSQNRVVCH YCGVAFPVPN
ACRECTGPLL KLGIGTERVE AEVLERMPHA RVARLDRDSA TSAEKLTELL ASFARREIDV
LVGTQMVAKG HDFPGVTLVC VVMADTSLAI PDFRAAERTF HLLTQVAGRA GRGKDPGRVL
VQTYNPDAEP VRRMLAHDFD GFSKQELEWR KALAYPPFAR MAAVRLEGEH PEQTAGVARF
LGNLVGRHMP PASAGVRLLG PALAPIARIR GKTRWQLLLK APTHAALAPL LARLEAALAD
VPNGVKVVID VDPGAML
//