ID A0A172TKB1_9BACL Unreviewed; 854 AA.
AC A0A172TKB1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=SY83_15650 {ECO:0000313|EMBL:ANE47478.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE47478.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE47478.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE47478.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) 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; CP011388; ANE47478.1; -; Genomic_DNA.
DR RefSeq; WP_068608191.1; NZ_CP011388.1.
DR AlphaFoldDB; A0A172TKB1; -.
DR STRING; 1178515.SY83_15650; -.
DR KEGG; pswu:SY83_15650; -.
DR PATRIC; fig|1178515.4.peg.3146; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000076927; 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:UP000076927};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 312..478
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 588..742
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 553..565
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 580..596
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 854 AA; 95924 MW; 96341F28FBF9C6CF CRC64;
MTYAKVIVDV PSKETNRPYD YVIPPKLSGW VEIGSRVGVP FGPRILQGFV VGLHQEAEVD
AARIKPIAEV SDSEPPLTPE LVKLSRWMSK TYLCHDITAL QAMIPGALKA KYERYIQAAE
GVTSPQSAVE HGVFAGGEMT GNGQGILFES ETLERESILR YVIAKGPVKT EQLLLKFEGQ
ATLIKQMLLS GQLTEAQVIK DRLSQKKVLT VYPNENKNEI RAYLDKLPAN AKRQKDVLDY
LLLHHEPVKL ADLLAELDLS ASTVKSLAEK GMLIIREADE FRNPYEGRDF TPTLPMLLTP
QQQIAYDAIR QDLDDRIHRT YLLQGVTGSG KTEVYLQTIQ RTLDAGREAI VLVPEISLTP
QMVERFKGRF GDQVAVLHSR LSQGERYDEW RKIRAGQVTV AIGARSAIFA PFTKIGLIII
DEEHESSYKQ EESPKYHAKR VAIERACAHD AVVVLGSATP SLETFYQTKS DLHGVPVRLS
GGEPAIRLIT MSERVAGRPM PEVKIVDLRE ELKAGNRSMF SRELYSAIET RLHKKEQTVL
LLNRRGYSTF VMCRSCGFVA GCPHCDISLT YHQRSRNLRC HYCGYAEREP EVCPDCKSEH
IRFFGTGTQK VEEELGKLFP GIRVIRMDVD TTTEKGSHEK WLTQFRNKEA DVLLGTQMVA
KGLDFPDVTL VGVIAADTVL NLPDFRAGEK TFQLLTQVAG RAGRHHLPGE VVIQSYSPEH
YSIEHASRHD YDSFVMQELG MRKERGYPPY CRLILITMSH EHIPVLVQIG EALANTLRER
AGAAREGEPS FEVMGPVASP IPRIKDRYRF QCMVKYREES AAIEAVKAVL ASFESRVKPH
KIQISVDVDP QILM
//
