ID E2ZCK5_9FIRM Unreviewed; 793 AA.
AC E2ZCK5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:EFQ04192.1};
GN ORFNames=HMPREF9429_01377 {ECO:0000313|EMBL:EFQ04192.1};
OS Megasphaera micronuciformis F0359.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ04192.1, ECO:0000313|Proteomes:UP000003195};
RN [1] {ECO:0000313|EMBL:EFQ04192.1, ECO:0000313|Proteomes:UP000003195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0359 {ECO:0000313|EMBL:EFQ04192.1,
RC ECO:0000313|Proteomes:UP000003195};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ04192.1}.
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DR EMBL; AECS01000037; EFQ04192.1; -; Genomic_DNA.
DR RefSeq; WP_006942551.1; NZ_GL538208.1.
DR AlphaFoldDB; E2ZCK5; -.
DR STRING; 706434.HMPREF9429_01377; -.
DR GeneID; 78569251; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_9; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000003195; 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; 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}; 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:UP000003195};
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 793 AA; 90382 MW; B8F8FA3276BE2E96 CRC64;
MIAHVIINIT AKGLQKTFTY LVPDSLKERI VIGARVLVPF GTRREEGIVV STEDELTQIP
EFKLKPIQAV LSVQPGKQDE IMATALWISQ YYVCNLADAL RLFFIEKHGI AYDYEVKLRA
EADIPAALTE AERQVLSSVS DRKEHRERDL LCRVDPQALD SLVNKGILLR SERVLNKIGP
KTKKWLRFIK TDVDKILARK KQQARLLSFL EEKKEASFDT LMEAGYGRAV INHLSETDFV
EVFYREKETV YLPTAAEKDE KWTLTAEQEA AVQAVETDAT SRTWVMRGVT GSGKTEVYMR
LAEKIIRKGK QVLLLVPEIA LTGQIVRRFT ARFANEVTVM HSQLSKGERE NNRRRMATGE
SAVCIGARSA VFTPFADLGL VIIDEEHDSS YKQDETPRYH AVEVARKRAS YYKAPVILGS
ATPSVNDYEK ALKGEYGLIE LKHRVLNRPL PEVEVVDMRQ ELEMQNYGVL SEKLKDLLKD
TLAAKRQAIV LLNRRGFSTF VMCRKCGYVV KCKTCDVPMV YHKQSEHLRC HYCEAVADIP
ERCPQCGSKY IKFFGAGTER VEAEIREFFP QARVVRLDQD TTVRKNSGDA IIEAFRRHEY
DILLGTQMVA KGHDFPNVAA VGILAADSLL NLPAYWAGER TFQLLTQAAG RAGRDRIPGK
VVMQTYAPEH YVIKHSRNQD YAGFFKEEIE FRRELSYPPF GKLVKITIID EDEKDLWRRG
NDLYERLNLY AKSEGAGDLE IIGPYVDIIK KIRNKFRIVI LIRALNPAPV KAFIHKDKAF
WKRGVLIDAD PNF
//
