ID A9BEB8_PROM4 Unreviewed; 753 AA.
AC A9BEB8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
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:ABX08428.1};
GN OrderedLocusNames=P9211_04971 {ECO:0000313|EMBL:ABX08428.1};
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08428.1, ECO:0000313|Proteomes:UP000000788};
RN [1] {ECO:0000313|EMBL:ABX08428.1, ECO:0000313|Proteomes:UP000000788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000878; ABX08428.1; -; Genomic_DNA.
DR RefSeq; WP_012195051.1; NC_009976.1.
DR AlphaFoldDB; A9BEB8; -.
DR STRING; 93059.P9211_04971; -.
DR KEGG; pmj:P9211_04971; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_0_3; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000000788; 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 GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
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 damage {ECO:0000256|ARBA:ARBA00023236};
KW 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:UP000000788};
KW SOS response {ECO:0000256|ARBA:ARBA00023236};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00983};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00983}.
FT DOMAIN 228..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 497..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ZN_FING 459..471
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
FT ZN_FING 489..505
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00983"
SQ SEQUENCE 753 AA; 83491 MW; 6FB04975C82F8034 CRC64;
MRLLEIDVWL EVGREGRTFS YGDSKQLGID LGDIVLVGLR GRRMHGLVVG KRVRQLNSEA
EQLSLKKKNF SLTDIESIVQ KAAVEPEWRE WVEASANKCH TGLFRMLKAA LPPGWLGSRN
LKSSEQKKYW WISLITPHDI DTELSFKQQK VVNFLQSRGG GSWQKDFVIE GISLSVLKSC
LARGVVSREK RNFLISRQST AIKPFLDKAN QESPRHLTDE QKIAMEAFFE QPPGSTFLLW
GVTGSGKTEV YLQIVAKELS EGRHCLILAP EIGLIPQLVD RLVKRFGPRV LEYHSGCTQN
ERVKAWREAL TTSQALVVVG TRSAVFLPLT PLGLIVLDEE HDSSYKQESP MPCYHARDLA
VDRAQRVGAK VLLGSATPSL ATWKDLSPRG PISFKRLTRR IANKPLPLVH VVDMRQELAY
GNRRLISKPL MDRLSALPAL GEQAVILVPR RGYSTFLSCR SCGEVVQCPN CDVSLTVHQG
RQGSQWLRCH WCDHRANIGF NCNQCGSKAF KPFGAGTQRV LEHLATELKE LKLLRFDRDS
TGGRDGHRRL LEKFAAGKAD VLVGTQMLAK GMDIPSVTLA VVLAADGLLH RPDLFAGEQS
LQLFMQLAGR AGRGEKKGKV FVQTYSPEHP VIKHLVDGCY ESFLKKEAKL RSEAGLVPYS
RACLLRVSGE TASVTATSAT ALAEYLKPFC KSNGWTIVGP APAMVERVAG KSRWQLLLHG
PQSSPLPIPS GGQLWSCLSK GVNLSIDPDP INL
//