RPOC_CHLTA
ID RPOC_CHLTA Reviewed; 1396 AA.
AC Q3KM48;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=CTA_0336;
OS Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=315277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT genitotropic strains.";
RL Infect. Immun. 73:6407-6418(2005).
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}.
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DR EMBL; CP000051; AAX50574.1; -; Genomic_DNA.
DR RefSeq; WP_009871661.1; NC_007429.1.
DR AlphaFoldDB; Q3KM48; -.
DR SMR; Q3KM48; -.
DR EnsemblBacteria; AAX50574; AAX50574; CTA_0336.
DR KEGG; cta:CTA_0336; -.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002532; 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; -; 1.
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..1396
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225523"
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 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1396 AA; 154905 MW; B24BF8841D284065 CRC64;
MFREGSRDDA ALVKEGLFDK LEIGIASDVT IRDKWSCGEI KKPETINYRT FKPEKGGLFC
EKIFGPTKDW ECYCGKYKKI KHKGIVCDRC GVEVTLSKVR RERMAHIELA VPIVHIWFFK
TTPSRIGNVL GMTASDLERV IYYEEYVVID PGNTDLVKKQ LLNDAKYREV VEKWGKDAFV
AKMGGEAVYD LLKSEDLESL LGELKERLRK TKSQQARMKL AKRLKIVEGF VSSSNRPEWM
VLKNIPVVPP DLRPLVPLDG GRFATSDLND LYRRVINRNN RLKAILRLKT PEVIVRNEKR
MLQEAVDALF DNGRHGHPVM GAGNRPLKSL SEMLKGKNGR FRQNLLGKRV DYSGRSVIIV
GPELKFNQCG LPKEMALELF EPFIIKRLKD QGSVYTIRSA KKMIQRGAPE VWDVLEEIIK
GHPVLLNRAP TLHRLGIQAF EPVLIEGKAI RVHPLVCAAF NADFDGDQMA VHVPLSIEAQ
LEAKVLMMAP DNIFLPSSGK PVATPSKDMT LGIYYLMADP TYFPEEHGGK TKAFKDEVEV
LRALNAGGFI LKDEICGSRR DETGRGIHIH EKIKVRIDGQ IIETTPGRVF FNTIVPKELG
FQNYSMPSKR ISELILQCYK KVGLEATVRF LDDLKELGFV QSTKAAISMG LKDVKIPEIK
KEILKDAYDK VAVVKKQYED GIITDGERHS KTISIWTEVS DLLSNALYSE IKKQTNSKHN
PLFLMIDSGA RGNKSQLKQL GALRGLMAKP NGAIIESPIT SNFREGLTVL EYSISSHGAR
KGLADTALKT ADSGYLTRRL VDVAQDVIIT ERDCGTLNHI EVSTIRQGSE ELLPLKDRVY
GRTVSENIYQ PGDKSNVLAY AGDVLTSAQA EAIDDAGIES VKIRSTLTCE SRRGVCAKCY
GLNLANGRLI GLGEAVGIIA AQSIGEPGTQ LTMRTFHLGG IAATSSTPEI VAECDGILVY
LDLRVVVDQE GNNLVLNKMG ALHLVQDEGR SLSEYKKLLS TKSIESLATF PVELGAKILV
NDGAAVAAGQ RIAEVELHNI PIICDKPGFV HYEDLVEGVS TEKVTNKNTG LVELIVKQHR
GELHPQIAIY ADANMKELVG TYAIPSGAII SVEEGQRIAP GMLLARLPRG AIKTKDITGG
LPRVAELVEA RKPEDAADIA KIDGVVDFKG IQKNKRILVV RDEITGMEEE HLISLTKHLI
VQRGDSVIKG QQLTDGLVVP HEILEICGVR ELQKYLVNEV QEVYRLQGVD INDKHVEIIV
RQMLQKVRIT DPGDTTLLFG EDVDKKEFYE ENRRTEEDGG KPAQAVPVLL GITKASLGTE
SFISAASFQD TTRVLTDAAC SSKTDYLLGF KENVIMGHMI PGGTGFDTHK RIKQHLEKEQ
EDLVFDFDSE FESVAG
