RPOC_TREPA
ID RPOC_TREPA Reviewed; 1416 AA.
AC O83270;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=TP_0242;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65230.1; -; Genomic_DNA.
DR PIR; D71350; D71350.
DR RefSeq; WP_010881690.1; NC_021490.2.
DR AlphaFoldDB; O83270; -.
DR SMR; O83270; -.
DR STRING; 243276.TPANIC_0242; -.
DR EnsemblBacteria; AAC65230; AAC65230; TP_0242.
DR KEGG; tpa:TP_0242; -.
DR eggNOG; COG0086; Bacteria.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000811; 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..1416
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067823"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 781
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 855
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 865
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1416 AA; 159790 MW; 78D0EB6A1CAF7C9C CRC64;
MKDIRDFDSL QIKLASPDTI RAWSYGEVKK PETINYRTLR PEREGLFCER IFGTTKEWEC
FCGKFKSIRY RGVICDRCGV EVTHFKVRRE RMGHIELATP VSHIWYYRCV PSRMGLLLDL
QVIALRSVLY YEKYIVIEPG DTDLKKNQLL TETEYNDAQE RYGGGFTAGM GAEAIRTLLQ
NLDLDALVAQ LREKMMEKGA KSDKRLLRRI EIVENFRVSG NKPEWMILSV IPVIPPDLRP
MVQLDGGRFA TSDLNDLYRR VIHRNSRLIR LMELKAPDII IRNEKRMLQE AVDALFDNSK
RKPAIKGASN RPLKSISDML KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLWQCGLPTK
MALELFKPFI MKKLVEKEIV SNIKKAKMLV EQESPKVFSV LDEVVKEHPV MLNRAPTLHR
LGIQAFEPVL VEGKAIRLHP LVCKPFNADF DGDQMAVHVP LTQAAQMECW TLMLSNRNLL
DPANGRTIVY PSQDMVLGLY YLTKERSLPE GARPRRFSSV EEVMMAAEKG VIGWQDQIQV
RYHKCDGQLV VTTAGRLVLN EEVPAEIPFV NETLDDKRIR KLIERVFKRQ DSWLAVQMLD
ALKTIGYTYA TFFGATLSMD DIIVPEQKVQ MLEKANKEVL AIASQYRGGH ITQEERYNRV
VEVWSKTSEE LTSLMMETLE RDKDGFNTIY MMATSGARGS RNQIRQLAGM RGLMAKPSGD
IIELPIRSNF KEGLNVIEFF ISTNGARKGL ADTALKTADA GYLTRRLVDI AQDVVVNEED
CGTINGIEYR AVKSGDEIIE SLAERIVGKY TLERVEHPIT HELLLDVNEY IDDERAEKVE
EAGVESVKLR TVLTCESKRG VCVCCYGRNL ARNKIVEIGE AVGIVAAQSI GQPGTQLTMR
TFHVGGTASS TTEENRITFK YPILVKSIEG VHVKMEDGSQ LFTRRGTLFF HKTLAEYQLQ
EGDSVQVRDR ARVLKDEVLY HTTDGQTVYA SVSGFARIID RTVYLVGPEQ KTEIRNGSNV
VIKADEYVPP GKTVATFDPF TEPILAEQDG FVRYEDIILG STLIEEVNTE TGMVERRITT
LKTGIQLQPR VFISDESGNA LGSYYLPEEA RLMVEEGAQV KAGTVIVKLA KAIQKTSDIT
GGLPRVSELF EARRPKNAAV LAQISGVVSF KGLFKGKRIV VVRDHYGKEY KHLVSMSRQL
LVRDGDTVEA GERLCDGCFD PHDILAILGE NALQNYLMNE IRDVYRVQGV SINDQHIGLV
VRQMLRKTEV VSVGDTRFIY GQQVDKYRFH EENRRVEAEG GQPAVARPMF QGITKAALNI
DSFISAASFQ ETNKVLTNAA IAGSVDDLCG LKENVIIGHL IPAGTGMRRY RQVKLFDKNK
RDLDVQMEEV IRRRKLEEEA LAQAVAGMEG EPEGEA
