RPOC_CHLPN
ID RPOC_CHLPN Reviewed; 1393 AA.
AC Q9Z999; Q9JSJ7; Q9K211;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
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};
GN OrderedLocusNames=CPn_0082, CP_0693, CpB0082;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) 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:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
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=AAF38501.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD18235.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38501.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000008; BAA98292.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98015.1; -; Genomic_DNA.
DR PIR; B86501; B86501.
DR PIR; E72122; E72122.
DR PIR; E81548; E81548.
DR RefSeq; NP_224290.1; NC_000922.1.
DR RefSeq; WP_010895278.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z999; -.
DR SMR; Q9Z999; -.
DR STRING; 115711.CP_0693; -.
DR PRIDE; Q9Z999; -.
DR EnsemblBacteria; AAD18235; AAD18235; CPn_0082.
DR EnsemblBacteria; AAF38501; AAF38501; CP_0693.
DR GeneID; 45050127; -.
DR KEGG; cpa:CP_0693; -.
DR KEGG; cpj:rpoC; -.
DR KEGG; cpn:CPn_0082; -.
DR KEGG; cpt:CpB0082; -.
DR PATRIC; fig|115713.3.peg.94; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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 Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
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; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
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;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1393
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067728"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 812
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 887
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT CONFLICT 1031
FT /note="A -> G (in Ref. 1; AAD18235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1393 AA; 154901 MW; E0734EF236C6FDE8 CRC64;
MFGENSRDIG VLSKEGLFDK LEIGIASDIT IRDKWSCGEI KKPETINYRT FKPEKGGLFC
EKIFGPTKDW ECCCGKYKKI KHKGIVCDRC GVEVTLSKVR RERMAHIELA VPIVHIWFFK
TTPSRIGNVL GMTASDLERV IYYEEYVVID PGKTDLTKKQ LLNDAQYREV VEKWGKDAFV
AKMGGEAIYD LLKSEDLQSL LKDLKERLRK TKSQQARMKL AKRLKIIEGF VSSSNHPEWM
VLKNIPVVPP DLRPLVPLDG GRFATSDLND LYRRVINRNN RLKAILRLKT PEVIVRNEKR
MLQEAVDALF DNGRHGHPVM GAGNRPLKSL SEMLKGKNGR FRQNLLGKRV DYSGRSVIIV
GPELKFNQCG LPKEMALELF EPFIIKRLKD QGSVYTIRSA KKMIQRGAPE VWDVLEEIIK
GHPVLLNRAP TLHRLGIQAF EPVLIEGKAI RIHPLVCAAF NADFDGDQMA VHVPLSVEAQ
LEAKVLMMAP DNIFLPSSGK PVAIPSKDMT LGLYYLMADP TYFPEEHGGK TKIFKDEIEV
LRALNNGGFI DDVFGDRRDE TGRGIHIHEK IKVRIDGQII ETTPGRVLFN RIVPKELGFQ
NYSMPSKRIS ELILQCYKKV GLEATVRFLD DLKDLGFIQA TKAAISMGLK DVRIPDIKSH
ILKDAYDKVA IVKKQYDDGI ITEGERHSKT ISIWTEVSEQ LSDALYVEIS KQTRSKHNPL
FLMIDSGARG NKSQLKQLGA LRGLMAKPNG AIIESPITSN FREGLTVLEY SISSHGARKG
LADTALKTAD SGYLTRRLVD VAQDVIITEK DCGTLNHIEI SAIGQGSEEL LPLKDRIYGR
TVAEDVYQPG DKSRLLAQSG DVLNSVQAEA IDDAGIETIK IRSTLTCESP RGVCAKCYGL
NLANGRLIGM GEAVGIIAAQ SIGEPGTQLT MRTFHLGGIA ATSSTPEIIT NSDGILVYMD
LRVVLGQEGH NLVLNKKGAL HVVGDEGRTL NEYKKLLSTK SIESLEVFPV ELGVKILVAD
GTPVSQGQRI AEVELHNIPI ICDKPGFIKY EDLVEGISTE KVVNKNTGLV ELIVKQHRGE
LHPQIAIYDD ADLSELVGTY AIPSGAIISV EEGQRVDPGM LLARLPRGAI KTKDITGGLP
RVAELVEARK PEDAADIAKI DGVVDFKGIQ KNKRILVVCD EMTGMEEEHL IPLTKHLIVQ
RGDSVIKGQQ LTDGLVVPHE ILEICGVREL QKYLVNEVQE VYRLQGVDIN DKHIEIIVRQ
MLQKVRITDP GDTTLLFGED VNKKEFYEEN RRTEEDGGKP AQAVPVLLGI TKASLGTESF
ISAASFQDTT RVLTDAACCS KTDYLLGFKE NVIMGHMIPG GTGFETHKRI KQYLEKEQED
LVFDFVSETE CVC
