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Database: UniProt
Entry: R5CG95_9FIRM
LinkDB: R5CG95_9FIRM
Original site: R5CG95_9FIRM 
ID   R5CG95_9FIRM            Unreviewed;       760 AA.
AC   R5CG95;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ORFNames=BN785_01081 {ECO:0000313|EMBL:CCX63822.1};
OS   Firmicutes bacterium CAG:791.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262993 {ECO:0000313|EMBL:CCX63822.1, ECO:0000313|Proteomes:UP000018038};
RN   [1] {ECO:0000313|EMBL:CCX63822.1, ECO:0000313|Proteomes:UP000018038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:791 {ECO:0000313|Proteomes:UP000018038};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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}.
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:CCX63822.1}.
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DR   EMBL; CAWT010000029; CCX63822.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5CG95; -.
DR   STRING; 1262993.BN785_01081; -.
DR   Proteomes; UP000018038; 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:UP000018038};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT   DOMAIN          228..394
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          490..655
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         456..468
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT   ZN_FING         482..498
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   760 AA;  85859 MW;  2F13AAD2EEA68FFF CRC64;
     MTYCYAQIII DISHGRLDRP FTYRIPEALQ NDLCLGSLVV VPFGKGDTKR KGYVIGFSNT
     CEYPDGKLKE IEAIASGGTD VTGDNAVRLA LWMKQRYGST MAVALRTVLT SRKQAKPCEH
     RSIHLLLSKD DAEKKRHEFA MKHQVARERL LRELMEAPDQ PYSLIIQKLH VTAPVIAALK
     KQGILEVRTE MFLRNPVSIE KCEEAGIRLS PEQRAISEGV LQDFEALQEG KNIPRVSLIH
     GITGSGKTEV YIAIIEEIVK RGRQAIMLIP EISLTYQTLM RFYRHFGDRV SVMNSTLSES
     EKSDQFERAR RGEIDVIIGP RSALFTPFPR IGAIIMDEEH ESSYKNESMP KYHTREVAEK
     IASMQNGVVV LGSATPSLES YYQAKEGKYR LYELSRRLTG GTLPSVEITD LREELRAGNH
     SILSRRLSEL VSDRLAKGQQ TMLFLNRRGF SGFVSCRSCG FVPKCPHCSV SLSLHRGGRL
     LCHYCGYEEP MPDKCPECGS PYISGFHAGT EQAESFLSRQ FPKARILRMD ADTTRTKGSY
     EKILSSFANE EADILIGTQM IVKGHDFPNV TLVGILLADQ SLNASDYRSA ERTFQLLTQA
     AGRAGRGKYP GDVVIQTYEP EHYSIVHAAH QNYEEFYREE MVYRKLLRYP PAEHLLAIQI
     ISRSEEHASL FAHKTRALLE QLTVAAREKN PDRLLFIGPA PAVLEKLRDE YRYVIYVKSP
     DYDTLIVCKD GVEAAAERAV KASREMDTMF QFDFDPINAF
//
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