RPOC_ACHLI
ID RPOC_ACHLI Reviewed; 1375 AA.
AC A9NEL8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=ACL_0172;
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Acholeplasma.
OX NCBI_TaxID=441768;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A;
RX PubMed=21784942; DOI=10.1128/jb.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
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 1 Zn(2+) ion per subunit; 2 are expected compared to other
CC organisms. {ECO:0000305};
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, ECO:0000305}.
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DR EMBL; CP000896; ABX80798.1; -; Genomic_DNA.
DR RefSeq; WP_012242129.1; NC_010163.1.
DR AlphaFoldDB; A9NEL8; -.
DR SMR; A9NEL8; -.
DR STRING; 441768.ACL_0172; -.
DR PRIDE; A9NEL8; -.
DR EnsemblBacteria; ABX80798; ABX80798; ACL_0172.
DR GeneID; 66293169; -.
DR KEGG; acl:ACL_0172; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008558; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1375
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353468"
FT REGION 1..158
FT /note="Unknown"
FT REGION 159..1353
FT /note="DNA-directed RNA polymerase subunit beta'"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 607
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 609
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1375 AA; 155620 MW; 97479A0722DB18FE CRC64;
MAKNEVLSLP VDSLKLSQTA LDRLKLSGIS RLEDFNTFNL KELQMLLSDS FNEVLPTLIY
YKLPRDVRDL SLSDEVVSVL ETAGIKDLEA LTKYDKSTLY HVFKDDEFLL KEINDLFELY
HEEKLSTLNV ATEVFEEVAL PQEVSVEDRV NKIIQPIRKT YGSKAFTHFK VRLASPDEIR
NWSYGEVINH ETINYRTSKP EPGGLFDERI FGPTRDYQCA CGKKQTVNKG QICPKCGIEI
TESKVRRERM GHINLEAPVV HTWYLKNSPS RLAILLGIKA KQLEEVVYHA SYIVTDPGQN
TPLAKKQILS EQDYSLLVEE YGSRFTALTG AEAVKKLLQD LDLDKEVKNL RKRLKTSSKQ
KRDRIIKRLD VVEAFNQSDN KPEWMVMDVI PVIPPDLRPM VPLDGGRFAT TDLNDLYRRI
LNRNNRLKKQ KEQMAPRLIT KNEKRMLQEA VDALFDNAKR GKKAAVERNR HLKSLSDLLR
GKQGRFRQNL LGKRVDYSGR SVIIVGPDLE MYQCGIPREM AITLFKPFIL RELQLTHGAE
KKNANAKYER RDDDTWRALE KVVREHPVLL NRAPTLHRLG IQAFEVKLID GKAIRLHPLV
TPAFNADFDG DQMAVHLPLS PEAQAEARLL MLASNNILNP RDGKPVVTPS QDMVLGNYYL
TIEESKDRNF GDDLERTKKH QEKHRHEGKF FSSIDEVKIA YENKDISLHT RIIIKPESVK
DTFTVEQKNM YLVTTLGKII FNEILPETFP YVNEPTMSNL SEKTPDIYFI KKGVNPKDAL
KHIPTPEPFK KRFLSMVIAQ VFKLFHISET SRMLDKLKDL GFKYSTVAGI TISYADINVY
SKKKEMVEAT EEEINEIEEW FEDGLLTDSE RRKLVIDKWT NVKNEIQSGI MKEFDKDNNI
FMMSDSGARG NVSNFTQLVG MRGLMSNPKG ETIEVPVQSS FREGLTVSEF FISTHGARKG
STDTALKTAE SGYLTRRLVD VSQDVIIVED DCGSSHGVYV EAIKDESGKE IVPLYDRIYG
RFAAHDIISP KTGEVFVKRN ELITEEIGLA IVKSGMQKVE IRSIMTCTSS HGICAKDYGI
NLATNQFVEV GEAIGVVAAQ SIGEPGTQLT MRTFHTGGVA AGADITQGLP RIQELFEARN
PKGKATISEV EGKVKDISRR GGSISITITD TQGTEYKYTL DPNIEALVKK GQDVVAGQKL
SSGSINPKEL LRVTDVKTAS NYILEEVQKV YRAQGVEISD KHVEVIIRQM LRRIMVIIEG
DTNILPGTEV SIDEFKRENK EVLKNRGRLA VGRPILLGIT RASLRSDSFL SAASFQETTR
ILTDAAIRSK KDELHGLKEN VIIGGLIPAG TGILQEKFFH YDQPEDKKPI YDDFE
