RPOC_PARUW
ID RPOC_PARUW Reviewed; 1388 AA.
AC Q6MDM0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=pc0605;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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; BX908798; CAF23329.1; -; Genomic_DNA.
DR RefSeq; WP_011175155.1; NC_005861.1.
DR AlphaFoldDB; Q6MDM0; -.
DR SMR; Q6MDM0; -.
DR STRING; 264201.pc0605; -.
DR PRIDE; Q6MDM0; -.
DR EnsemblBacteria; CAF23329; CAF23329; PC_RS02900.
DR KEGG; pcu:PC_RS02900; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000529; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1388
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225559"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
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 1388 AA; 155297 MW; 3803E1C156B9F77D CRC64;
MSERNQQDGQ FDKLTIKIAS DDVIRNEWSR GEIKKPETIN YRTFKPEKGG LFCEKIFGPT
RDWECACGKY KKIKHKGIVC DRCGVEVTLS KVRRERMAHI DLAVPVVHIW FFKTMPSRIG
NVLGMTSADL ERVIYYEEYV VINPGQTDLE RKQLLNDTEY REAQEKWGRD SFVAKMGGEA
IRDLLASEDL QTQLVELKDK LRKTKSQQAR MKLAKRLKII ESFVSSDNKP EWMIMSCVPV
IPPDLRPLVP LDGGRFATSD LNDLYRRVIN RNNRLKAILK LKTPDVIVRN EKRMLQEAVD
ALFDNGRHGH PVMGAGNRPL KSLSEMLKGK QGRFRQNLLG KRVDYSGRSV IIVGPELKFN
QCGLPKLMAL ELFEPFIVKR LKDQGYVYTI RSAKKMIQRH APEVWDVLED IIKGHPVLLN
RAPTLHRLGI QAFEPVLIEG KAIRIHPLVC SAFNADFDGD QMAVYVPLSI EAQLEAKLLM
MAPDNIFLPS SGKPVAVPSQ DMTLGLYYLM LDPLYIRENH ELKTRVFRDS EEVLLALQAS
GSYNWYEEGS KSPNGENRSD YLRGIRIHEK IKLRTENGII ETTPGRVVFN TIVPKELGFQ
NYSLPKKKMG ELVMQCYKKA GLEATVRFLD NLKSIGFAEA TKSALSMGVC DVKIPTIKQK
ILHDAHERVA VVRKQYEDGI ITEGERYSKT ISIWTEVSDV LSEELFKLIS EVKDSTMNPL
YLMMDSGARG NKSQIRQLGA LRGLMAKPSG DIIESPITSN FREGLSVIEF SISSHGARKG
LADTALKTAD SGYLTRRLVD VAQDVIITED DCGTLNGIDV SAIKQGQEEL LPLKDRIFGR
TVCEDIYQPG DSTKLLAKSG DTLTVLQAEA IDDSGIESIR IRSVLTCETR RGVCAKCYGI
NLANSRSISM GEAVGIIAAQ SIGEPGTQLT MRTFHLGGIA SAGLTPEIVA DDNGILVYTD
LRTVKTDEGN WVALNKNGRL NIVKDEGRTL DEYKKLLSTK SIEPLQAFNV ELGTKILLEE
GTKVKPGTRV AEWEQHNIPI ICDRPGYVRY EDLVEGLSTE RDVNKQTGQA ELIVKQHRGE
LHPQVAIYAD QACEDLVGTY PLPAGAIISV EEGEFATAGK MLARLPRSAI KTKDITGGLP
RVAELFEARK PKDSAEIAKI DGVVDFRGVQ KNKRIVVVRD EMTGMEEEHL ISHTKHLIIQ
RGDHVVKGQQ LTDGLVIPHE ILDICGVREL QKYLVNQVQE VYRLQGVDIN DKHIEIIVRQ
MLKKVRVIDP GDTSLLYGEE VDKKEFEVEN QKVSQEGGKA AQATPVLLGI TKASLSTESF
ISAASFQDTT RVLTEAACAG KTDYLVGFKE NVIMGHIIPG GTGFDRHKRV KMFVDSEQEQ
GLEFNFAD
