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Database: UniProt
Entry: M4ZTD2_9FLAO
LinkDB: M4ZTD2_9FLAO
Original site: M4ZTD2_9FLAO 
ID   M4ZTD2_9FLAO            Unreviewed;       614 AA.
AC   M4ZTD2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:BAM99588.1};
GN   ORFNames=BPAA_296 {ECO:0000313|EMBL:BAM99588.1};
OS   Blattabacterium cuenoti BPAA.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=1229512 {ECO:0000313|EMBL:BAM99588.1, ECO:0000313|Proteomes:UP000011815};
RN   [1] {ECO:0000313|EMBL:BAM99588.1, ECO:0000313|Proteomes:UP000011815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPAA {ECO:0000313|EMBL:BAM99588.1,
RC   ECO:0000313|Proteomes:UP000011815};
RX   PubMed=23515978; DOI=10.1098/rsbl.2012.1153;
RA   Tokuda G., Elbourne L.D.H., Kinjo Y., Saitoh S., Sabree Z., Hojo M.,
RA   Yamada A., Hayashi Y., Shigenobu S., Bandi C., Paulsen I.T., Watanabe H.,
RA   Lo N.;
RT   "Maintenance of essential amino acid synthesis pathways in the
RT   Blattabacterium cuenoti symbiont of a wood-feeding cockroach.";
RL   Biol. Lett. 9:20121153-20121153(2013).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
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:0000256|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR002811};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|PIRNR:PIRNR002811};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00974}.
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DR   EMBL; AP012548; BAM99588.1; -; Genomic_DNA.
DR   RefSeq; WP_015429907.1; NC_020510.1.
DR   AlphaFoldDB; M4ZTD2; -.
DR   STRING; 1229512.BPAA_296; -.
DR   KEGG; blp:BPAA_296; -.
DR   PATRIC; fig|1229512.3.peg.292; -.
DR   eggNOG; COG0358; Bacteria.
DR   HOGENOM; CLU_013501_3_0_10; -.
DR   Proteomes; UP000011815; Chromosome.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR006295; DNA_primase_DnaG.
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; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR002811};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR002811};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          260..341
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   614 AA;  72128 MW;  E5F41600555990B4 CRC64;
     MISKETIKKI LSASCIEDVI GDFVKLKKSG FNYRGLSPFS NEKTPSLIVS PTKKIWKDFS
     SGKGGNIITF LMEHEHFTYE ESLRFLAKKY EIKMDHIDNN NHQEKEEYEK SYLIQDYAKR
     FFIYQLHFTK EGQNNGLNYF IQKRGFDINI IHKFELGYAP ISWNLLTINA LKKGFKIRDI
     KESGVTVFRK SNHFFDCFRK RVMFPIHSLS GRVIGFGGRS LDSRSFTTTK YINSSESKIF
     QKSKILYGLF QAKKNILKEN FCYLVEGYTD VISLHQSGIK NVVSSSGISL TVAQILLIKK
     FTKNIVLFYD GDRSGIKASL RGINMMLEQE MNLRILFISN GEDPDLISKK YSFSQFRDFV
     AKNSYNFVSF KQKIYEKIHK DDPIKKSFLV KNILNSISKI SNVIQKELYL QEASKVLNIR
     QKVLISELKK INKKNVQKPS TVQVKGNSRF FLKKNTLLLL EEKLIQLILN HGNQIIKKKE
     HNTTILEEVL HVFKCWNLRF SLNKNQEIFD QICLQKKRID LSQFLDKKNP KFYSLSKWDR
     KGIQVSYQKE RINQYISDIL LRYKSLCISK LIQKEIIHYQ NDLKKNKDRK AFLKKIMHLT
     DIKNELHKKL HRYV
//
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