ID B0BPX1_ACTPJ Unreviewed; 746 AA.
AC B0BPX1;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
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:ABY69606.1};
GN OrderedLocusNames=APJL_1050 {ECO:0000313|EMBL:ABY69606.1};
OS Actinobacillus pleuropneumoniae serotype 3 (strain JL03).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=434271 {ECO:0000313|EMBL:ABY69606.1, ECO:0000313|Proteomes:UP000008547};
RN [1] {ECO:0000313|EMBL:ABY69606.1, ECO:0000313|Proteomes:UP000008547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL03 {ECO:0000313|EMBL:ABY69606.1,
RC ECO:0000313|Proteomes:UP000008547};
RX PubMed=18197260; DOI=10.1371/journal.pone.0001450;
RA Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W.,
RA Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T.,
RA Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S.,
RA Zhao G.-P., Chen H.;
RT "Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of
RT serotype 3 prevalent in China.";
RL PLoS ONE 3:E1450-E1450(2008).
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; CP000687; ABY69606.1; -; Genomic_DNA.
DR AlphaFoldDB; B0BPX1; -.
DR KEGG; apj:APJL_1050; -.
DR HOGENOM; CLU_013353_3_1_6; -.
DR Proteomes; UP000008547; 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; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 222..388
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 466..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 447..459
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 474..490
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 746 AA; 84241 MW; B10622450668EAB4 CRC64;
MSFRFLLIMS KLVRVALPVP LHRYFDYLLP SFLSAVKGVR VEVPFGNQTK IGIVVDFPET
SDVPEDKLKP IKAVLDLEPI FDKEIWTLLR WAARYYHAPI GEVAINALPV KLRNGDSTER
SQPDYFAVTE AGRAALLSGE NKRAKKQQDL LAKLAEIANF FEKPAACSQS AWKGLLEKNY
IELVNVPFEP QHWQKKLQNR PLVNLQNRLV LNKQQSLVVS RLTVQNGFEA FLLNGVTGSG
KTEVYLQVIE EVLKRGEQVL VLVPEIGLTP QTVQRFKARF NVEIDVLHSN MNETERLNAW
LRVKNGESAI VIGTRSALFS QFEKLGLIII DEEHDSSFKQ QDGWRYHARD LAILRAKNLH
IPIILGSATP SLESVQNVQN GKFIELSLTA RAGNAQQAKQ QLIDLKTQRI TAGLSDRLLA
MMKRHLEQGN QVVLFLNRRG FAPVLLCHEC GWMCECDACE KPYTYHQKQK ILRCHHCASQ
RVIPRQCGHC GSTNLITTGV GTEQLEQVLS EQFPTYQISR IDRDSTARKG ALENHLNDIR
EGKSQILIGT QMLAKGHHFP NVTLVAIVNV DSALFSTDFR AEERLAQLYV QVAGRAGRAE
KQGEVVLQTH YPEHPLLKTL LEQGYLAFAQ EALKMRKVMG LPPFAAQVLL RATGKDNQQV
VNLLQNLTAY FQQKCTELGL QDIQLLPPFS APMAKKAGHY RWLLLIQHRS RGVLQQLIDQ
FDLDKANLGL QNNIRLTLDI DPQEIG
//
