ID I9AYX6_9FIRM Unreviewed; 810 AA.
AC I9AYX6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=FB4_3576 {ECO:0000313|EMBL:EIW18102.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW18102.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW18102.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW18102.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(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}.
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:EIW18102.1}.
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DR EMBL; AKVJ01000028; EIW18102.1; -; Genomic_DNA.
DR RefSeq; WP_007934665.1; NZ_AKVJ01000028.1.
DR AlphaFoldDB; I9AYX6; -.
DR PATRIC; fig|1149862.3.peg.2536; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000004324; 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; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 292..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 555..729
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 520..532
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 547..563
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 810 AA; 91477 MW; 8E572FA78725FDC7 CRC64;
MQRIAQVLIN ITTKNINKAF SYSIPDHLDY VDAGWRVLVP FGNRKLEGFV IDIIIEEDSN
RIELKPIIDI LDNDKWFDEH MMHTARWISE YYLCNLVDAM RLFIPGKSGV KSVVAYSVEM
EVDTETTLVA LSAKYPEYSQ VLSYIETHSP ILSVKLEKKF GPSVLKAIRY LVRNKIIIAE
SIAKKMGTHR YKTIMSLLMD AEATREQISK LAKKPAQCRL LQYLIDHGQL ASDELKKSNT
SHETVKKLVQ DGLIKLEKVQ VVRDSYADIC KAKNDISLTA EQQQVLEKIM PKMEARKFQS
FLLHGITGSG KTQVYIEAVA AARQKNRQAI VLVPEIALTS QIVSRFKARF GDDVVVMHSK
LSTGERYDAW QRLRGKQAGI VIGARSAIFA PLPDVGIIIM DEEHEFTYKQ EETPRYHTRQ
VAITRATLSG AVVIMGSATP AIETYFQTQM GQHTLLLMSK RIANANLPAV TIVDMREELR
KKRRSVISLP LQELLQETIS RGEQAIILLN RRGYATFVMC RECGHIVRCK HCDISLVYHS
VGKKLKCHYC QCIETVPDIC PECNSRYIRF FGTGTQKLQE EIVTLFPHIR VVRMDQDTTG
GRMAYDRILE AFAKGEYDLL LGTQMVAKGH DVKNVTAVGI IAADSILNLP DFRAAERVYA
LLTQAAGRAG RGDKAGKVVV QTYNPEHYAV QAGANQDYQS FYESEIVYRK ALCYPPYGQI
IKLTVQAKEE SMARNQAEQI IKELRSLMAE SKTVEIIGPF PAPIAKVNDI FRMNIIIKAK
DLTNVRAYIT SMGLTIRPDV MIDVEPVSIM
//
