(data stored in ACNUC7421 zone)

SWISSPROT: RPOC_LEGPC

ID   RPOC_LEGPC              Reviewed;        1401 AA.
AC   A5IHS0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   11-DEC-2019, entry version 72.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=LPC_3020;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400;
CC         EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01322};
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC       and 1 omega subunit. When a sigma factor is associated with the core
CC       the holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_01322}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ56920.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; CP000675; ABQ56920.1; ALT_INIT; Genomic_DNA.
DR   SMR; A5IHS0; -.
DR   PRIDE; A5IHS0; -.
DR   EnsemblBacteria; ABQ56920; ABQ56920; LPC_3020.
DR   KEGG; lpc:LPC_3020; -.
DR   HOGENOM; HOG000218386; -.
DR   KO; K03046; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.274.100; -; 2.
DR   HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR   InterPro; IPR012754; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR038120; Rpb1_funnel_sf.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   SMART; SM00663; RPOLA_N; 1.
DR   TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IHS0.
DR   SWISS-2DPAGE; A5IHS0.
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT   CHAIN           1..1401
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353386"
FT   METAL           70
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           72
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           85
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           88
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           460
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           462
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           464
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           808
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           882
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           889
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   METAL           892
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1401 AA;  155626 MW;  556CCE9C38E40638 CRC64;
     MSDLLGILKQ QGQSEEFDAI KIALASPELI RSWSYGEVKK PETINYRTFK PERDGLFCAK
     TFGPVKDYEC LCGKYKRLKH RGVICEKCGV ELALAKVRRE RMGHIELASP VAHIWFLKSL
     PSRIGLLLDM TLRDIERVLY FEAFVVVDPG MTELERGQLL NDEAYLDAME QYGDEFDARM
     GAEAIRDLLR QIDLEDEIRN LREELPTTNS ETKIKKITKR LKLLEAFYES GNKPEWMIMD
     VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLNAPDI IVRNEKRMLQ
     ESVDALLDNG RRGRAITGTN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVIVVGPT
     LKLHQCGLPK KMALELFKPF IFSKLEFRGL ATTIKAAKKM VEREESVVWD ILDDVIREHP
     ILLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAYNAD FDGDQMAVHV PLTLEAQLEA
     RSLMMSTNNI LSPASGEPII VPSQDVVLGL YYLTREKVNA LGEGKIYSSA QEAQNFYEAG
     HLDIHAKIKI RMPKEDGETG YHLVETTVGR AILAEILPKG MPFDYINRTM TKKVISKVID
     SCYRKFGLKE TVIFADQLMY TGFKYATRSG ASIGIEDMEI PDDKASIIEH ADNEVREIES
     QFRSGLVTNG ERYNKVIDIW SRTNELVAKS MMSKIATEEV TDAKGNKVRQ ESFNPIFMMA
     DSGARGSAAQ IRQLAGMRGL MAAPDGSIIE TPITANFREG LNVFQYFIST HGARKGLADT
     ALKTANSGYL TRRLVDVAQD VVITEDDCGT DTGILMQPLI EGGDIVEPLH ERVLGRVVAS
     DVYIPTQTEP VVKAGTLLDE EWVEKLEKHG VDQVMVRSPI TCQTRFGLCA KCYGRDLARG
     HLVNTGEAVG IIAAQSIGEP GTQLTMRTFH IGGAASRATA ANNIQIKTKG VIRLHNIKTV
     THENKNLVAV SRSGEVTIVD EFGRERERYK VPYGAVISAQ DNSPVEAGQV IATWDPHTHP
     VISEVSGRLK FVDLIDGITM NRQTDELTGL SNIVIIDAKQ RSAAGRDLRP MVKLVTDEGD
     DIYLAGTNVP AQYYLPVDAI VNFEDGSLVG IGDVIARIPQ ERSKTRDITG GLPRVADLFE
     ARKPKDSAVM AEVSGLVNFG KETKGKRRLI INVSEDQCHE ELIPKWRHIS VFEGEHVERG
     EIIAEGALNP HDILRLLGVG ALANYIVNEV QDVYRLQGVK INDKHIEVIV RQMLRKRVIT
     FAGDSKFLVG EQVEESAMLQ ENDKLLAEGK QIARGTPILL GITKASLATE SFISAASFQE
     TTRVLTEAAV SGKVDELRGL KENVMVGRLI PAGTGYTYHQ SRKAKRARAA AGGDSSATHT
     VTASDVEHAL SEALNADNHE H
//

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