ID DNAG_PSEAE Reviewed; 664 AA.
AC Q9I5W0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; OrderedLocusNames=PA0577;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_00974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC domain that contains the primase activity, and a C-terminal DnaB-
CC binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; AE004091; AAG03966.1; -; Genomic_DNA.
DR PIR; E83572; E83572.
DR PIR; S15899; S15899.
DR RefSeq; NP_249268.1; NC_002516.2.
DR RefSeq; WP_003099594.1; NZ_QZGE01000010.1.
DR PDB; 5VAZ; X-ray; 2.40 A; A/B=106-486.
DR PDBsum; 5VAZ; -.
DR AlphaFoldDB; Q9I5W0; -.
DR SMR; Q9I5W0; -.
DR STRING; 208964.PA0577; -.
DR PaxDb; 208964-PA0577; -.
DR GeneID; 882047; -.
DR KEGG; pae:PA0577; -.
DR PATRIC; fig|208964.12.peg.612; -.
DR PseudoCAP; PA0577; -.
DR HOGENOM; CLU_013501_5_4_6; -.
DR InParanoid; Q9I5W0; -.
DR OrthoDB; 9803773at2; -.
DR PhylomeDB; Q9I5W0; -.
DR BioCyc; PAER208964:G1FZ6-584-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR Gene3D; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
DR InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR InterPro; IPR030846; DnaG_bac.
DR InterPro; IPR013264; DNAG_N.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR NCBIfam; TIGR01391; dnaG; 1.
DR PANTHER; PTHR30313; DNA PRIMASE; 1.
DR PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08278; DnaG_DnaB_bind; 1.
DR Pfam; PF08275; DNAG_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR SMART; SM00766; DnaG_DnaB_bind; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF117023; DNA primase DnaG, C-terminal domain; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Primosome;
KW Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..664
FT /note="DNA primase"
FT /id="PRO_0000180512"
FT DOMAIN 262..344
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 40..64
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT REGION 94..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5VAZ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5VAZ"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5VAZ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 262..269
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:5VAZ"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 349..368
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 372..383
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 409..423
FT /evidence="ECO:0007829|PDB:5VAZ"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:5VAZ"
SQ SEQUENCE 664 AA; 74176 MW; 8D149A92619214ED CRC64;
MAGLIPQSFI DDLLNRTDIV EVVSSRIQLK KTGKNYSACC PFHKEKTPSF TVSPDKQFYY
CFGCGAGGNA LGFVMDHDQL EFPQAVEELA KRAGMDVPRE ERGGRGHTPR QPTDSPLYPL
LSAAAEFYKQ ALKSHPARKA AVNYLKGRGL TGEIARDFGL GFAPPGWDNL LKHLGGDNLQ
LKAMLDAGLL VENSDTGKRY DRFRDRVMFP IRDSRGRIIA FGGRVLGDDK PKYLNSPETP
VFHKGQELYG LYEARQKNRD LDEIMVVEGY MDVIALAQQG IRNAVATLGT ATSEEHIKRL
FRLVPSILFC FDGDQAGRKA AWRALESVLP NLQDGKRVRF LFLPEGEDPD SLVRAEGEDA
FRARITQQAQ PLAEYFFQQL MLEADPATLE GKAHLATLAA PLLEKIPGNN LRLLMRQRLS
EITGLSGENI GQLAHHSPPP SSMDHGASGV LDGDDYFAAS AYYENEPSHA PFDAAPGYVE
AQPRKSWNKD KKPWDGKKWD GKKKWDKGGR GDFKAPQRTP VSVESTTLNA LRTLLHHPQL
ALKVDDAGTL AREQDTYAQL LVSLLEALQK NPRQSSMQLI ARWHGTPQGR LLQALGEKEW
LIVQENLEKQ FFDTITKLSE SQRFGEREER LRSVMQKSYS ELTDEEKALL REHYSVAASS
PSQS
//
