RPOC_ALIB4
ID RPOC_ALIB4 Reviewed; 1511 AA.
AC A8EVZ3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, 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=Abu_1883;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV68116.1; -; Genomic_DNA.
DR RefSeq; WP_012147822.1; NC_009850.1.
DR AlphaFoldDB; A8EVZ3; -.
DR SMR; A8EVZ3; -.
DR STRING; 367737.Abu_1883; -.
DR EnsemblBacteria; ABV68116; ABV68116; Abu_1883.
DR KEGG; abu:Abu_1883; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_7; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001136; 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..1511
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353289"
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 77
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 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1511 AA; 168145 MW; E40765D0276E8962 CRC64;
MSNNEKVLSP IEIKELERPQ DFSAFQLKLA SPEKILSWSC GEVKKPETIN YRTLKPERDG
LFCAKIFGPV KDYECLCGKY KKMRYKGVVC EKCGVEVTSS KVRRHRMGHI ELVSPVAHIW
MVSSLPTRIG TLLGVKLKDL ERVLYYEAYI VSNPGEAYYD NEKTKKVEKY DILNEEQYRT
ISDLFEHTGF EANMGGEIVR DLLAGLDLFE LLTLLKEEME TTKSEAKRKT IIKRLKVVEN
FLNSGNRPEW MMLTQLPVLP PDLRPLVSLD GGKFAVSDVN DLYRRVINRN NRLKRLTELD
APEIIIRNEK RMLQEAVDAL FDNGKTANAV KGANKRPLKS LSEIIKGKQG RFRQNLLGKR
VDFSGRSVIV VGPSLNMDQC GIPKKMALEL FKPHLMAKLE EKGYATTLKA AKRLIENESN
EVWECLNEIV DEYPILLNRA PTLHKLSIQA FHPVLIDGKA IRLHPLVCAA FNADFDGDQM
AVHVPLSQEA VAEAKILMMS SMNILLPASG RAIAVPSQDM ILGIYYLSLV KEGVKGEHKL
FTDVNEVKIA LDMGQIDLHA KIRTRIGDRI IQTTVGRLII HEILPSFVPA NLWNKILKKK
DIGILVDYIY KEAGYEVTPR FLDDLKNLGF KYATIAGISI SIDDIRVPEN KIMHISKSKK
DVIEVQKQFS QGLLTEQERY NKIIDIWTEV NNKLASEMME LVKGDKNGFN SIYMMADSGA
RGSAAQIRQL SGMRGLMAKP DGSIIETPII SNFREGLNVL EYFISTHGAR KGLADTALKT
ANAGYLTRKL IDVSQNVRIT IEDCGTHEGI EITDITSGNE LIESLEERIT GRVIAEDIID
PISNEILFAE GTLITEEDAK VVTEAEVKSV VIRTPLTCKV ENGLCSKCYG LNLGEQRKAK
PGEAVGVVAA QSIGEPGTQL TLRTFHVGGT ASATQTEREL KADKEGFIRY YNIKKYVTTD
GKIIVANRRN AGLLLVEPKI NAPFKGKVTV ETVHEEIILT IANSTEEKKY FLRKNDVAKA
NELAGISGKI EGKLYLPYKD GEEVNLNESI VEIIKDGWNV PNRIPFASEL KVEDGAPVTS
KIITGAKGIV KYYKLTGDYL ERRHDIKAGD IITEKGLFAV IADTEDREAL RHYISRGSCI
ALNDNTEVEK DTVISAPAKN EQVVIAEWDP YANPTIAEKA GVISFEDVIP GVTVSEQFDE
LTGTSKLVIN EYIPSGYKPT VILTTDDNEI IRYSLDPKIS LNVSEGKRVE VADIIGKTPK
ATQKSKDITG GLPRVSELFE ARRPKNIAIL ASFDGVVSFG KGLRNKQKIL ITDSTGNSVE
YLVEKSKQVL VHEGEFVHAG EALTDGQISP HDILRILGEK ALHYFIVSEV QQVYRSQGVN
IADKHIEVIT SQMLRQVSIL DGGDTKFIVG DMISKKKFKL ENEKIIKLGG NPAIAEPLLL
GITRAAVTSD SIISAASFQE TTKVLTEAAI SAKMDMLEDL KENVVIGRTI PVGTGLYKDQ
KVKFSEQEIS K
