RPOC_CHLAB
ID RPOC_CHLAB Reviewed; 1393 AA.
AC Q5L5I4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=CAB660;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(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; CR848038; CAH64107.1; -; Genomic_DNA.
DR RefSeq; WP_011097243.1; NC_004552.2.
DR AlphaFoldDB; Q5L5I4; -.
DR SMR; Q5L5I4; -.
DR PRIDE; Q5L5I4; -.
DR EnsemblBacteria; CAH64107; CAH64107; CAB660.
DR KEGG; cab:CAB660; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001012; 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..1393
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225524"
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"
SQ SEQUENCE 1393 AA; 154963 MW; 8EEB514CD278DB77 CRC64;
MFGEGSRDNV ALSKEGLFDK LEIGIASDIT IRDKWSCGEI KKPETINYRT FKPEKGGLFC
EKIFGPTKDW ECCCGKYKKI KHKGIVCDRC GVEVTLSKVR RERMAHIELA VLIVHIWFFK
TTPSRIGNVL GMTASDLERI IYYEEYVVID PGKTDLNKKQ LLNDAQYREV IEKWGKDSFV
AKMGGEAIYD LLKSEDLQSL LKELKDRLRK TKSQQARMKL AKRLKIIEGF VSSSNHAEWM
VLKSVPVVPP 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 TYFPEDHGGK IKIFKDVTEV
LRALYSGGFL DEHTDGRRDE TGRGIHIHEK IKVRIDGQVI ETTPGRVLFN RIVPKELGFQ
NYSMPSKRIS ELILQCYKKV GLEATVRFLD DLKDLGFIQA TKAAISMGLK DVKIPEIKSE
ILKEAYDKVA IVKKQYDDGI ITDGERHSKT ISIWTEVSEL LSDALYVEIS KQTKSKHNPL
FLMIDSGARG NKSQLKQLGA LRGLMAKPNG AIIESPITSN FREGLTVLEY SISSHGARKG
LADTALKTAD SGYLTRRLVD VAQDVIITEK DCGTLNHIEI TAIRQGSEEL LPLKDRIYGR
TVSEDIYQPG DKSKLLAENG DVITSAQAEL IDDAGIESIK IRSTLTCESR RGVCAKCYGL
NLANGRLIGL GEAVGIIAAQ SIGEPGTQLT MRTFHLGGIA ATSSTPEIVT NCDGILVYID
LRVVVGQDGN HLVLNKKGAI HVVRDEGRSL EEYKKLLSTK SIESLETYPV ELGVKILVGD
GEKVTAGQRI AEVELHNIPI ICDKPGFVKY EDLVEGISTE KVANKNTGLV ELIVKQHRGE
LHPQIAIYSD PGLTELVGTY AIPSGAIVSV EENQKVDPGM LLARLPRGAI KTKDITGGLP
RVAELVEARK PEDAADIAKI DGVVDFKGIQ KNKRILVVRD EITGMEEEHL IPLTKHLIVQ
RGDHVMKGQQ LTDGLVVPHE ILEICGVREL QKYLVNEVQE VYRLQGVDIN DKHVEIIVRQ
MLQKVRITDP GDTTLLFGEE VNKKEFYEEN KRTEEEGGKP AQAVPVLLGI TKASLGTESF
ISAASFQDTT RVLTDAACSS KTDYLLGFKE NVIMGHMIPG GTGFDTHKRI KQYLEKEQEE
LVFDFVSESE CAC
