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Database: UniProt
Entry: R5AK60_9FIRM
LinkDB: R5AK60_9FIRM
Original site: R5AK60_9FIRM 
ID   R5AK60_9FIRM            Unreviewed;       812 AA.
AC   R5AK60;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=BN453_00675 {ECO:0000313|EMBL:CCX39736.1};
OS   Firmicutes bacterium CAG:102.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1262998 {ECO:0000313|EMBL:CCX39736.1, ECO:0000313|Proteomes:UP000018112};
RN   [1] {ECO:0000313|EMBL:CCX39736.1, ECO:0000313|Proteomes:UP000018112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:102 {ECO:0000313|EMBL:CCX39736.1,
RC   ECO:0000313|Proteomes:UP000018112};
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:CCX39736.1}.
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DR   EMBL; CAWG010000041; CCX39736.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5AK60; -.
DR   STRING; 1262998.BN453_00675; -.
DR   Proteomes; UP000018112; 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:UP000018112};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT   DOMAIN          291..457
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          554..708
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   ZN_FING         519..531
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT   ZN_FING         546..562
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   812 AA;  91376 MW;  A54079021BECF6F3 CRC64;
     MMYAKVIVGL NQPEMDKLFD YRIPEGMTVE IGVRVIVPFG SRNKKAEGYV ISLSEKTEVP
     ADKIKELLEV LDEGRPTFTP ALLDLAEWMK ERYFCTLNQC LQAIMPPGIR TKSSWTVGRK
     SLDAETKLTP KETALLALFG ERREIPLEEV QAEFGGDCLT FLRKAEGKGL LALKQELHRS
     EYKNEKRLYS LDRDHPLLEA AWKKAEKEKR LEGQRLLLEY LANGREATVA ELKEALGITD
     SPIKTLLKKG ILRERRQTER RNVFDADTVE RTQPFTPTAE QAAALSVLHR ELEQEEKKPI
     LLHGVTGSGK TEIYMQIIAE VLTRGEQAIV LVPEIALTPL LAERFVSRFG AAVSVTHSRL
     SMGERVDQWK KARDGEISVV IGARSALFLP FPKVGAIIMD EAHENSYVSD ITPKYDTKDV
     AAALAKRYGA LFLMGTATPD FISYYKAKQG EFLLLELKER TGGGVLPRML VTDMRKELAE
     GNRSAFGRAL QEEIRRNLEK GEQTMLFLNR RGYATFVSCR SCGHVMKCPE CDLTYTYHAK
     EHALACHYCG RRAPLPKVCP VCGSKYIRYF GTGTQKIEEE ARKLFPEARI LRMDLDTTLT
     KHSHEKILAA FAAGEADILI GTQMIAKGHD YPNVTLVGIM AADLSLNADS FTAAETSFRL
     MLQAAGRAGR RDDRGRVFLQ TYQPQHYAVQ YAAKQDYEGF YEEEMLMRQM MGYPPFSAFF
     SILLTGAAQE EVAQAAQELA ERLAQADEEE IATILGPTAL PKFRGEYRCQ IIVKAAEEEP
     LRQLVLPTVE RMKKERSRNV RVGLALNPTN IV
//
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