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RPOC_ALCBS
ID   RPOC_ALCBS              Reviewed;        1400 AA.
AC   Q0VSM1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=ABO_0379;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15827.1; -; Genomic_DNA.
DR   RefSeq; WP_011587674.1; NC_008260.1.
DR   AlphaFoldDB; Q0VSM1; -.
DR   SMR; Q0VSM1; -.
DR   STRING; 393595.ABO_0379; -.
DR   PRIDE; Q0VSM1; -.
DR   EnsemblBacteria; CAL15827; CAL15827; ABO_0379.
DR   KEGG; abo:ABO_0379; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_6; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000008871; 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..1400
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000308817"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
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         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         814
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         889
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         899
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1400 AA;  155525 MW;  141487AD7999FC5E CRC64;
     MKDLLNLLKS QGQVTEFDKI RIALAPPDLI RSWSFGEVKK PETINYRTFK PERDGLFCAR
     IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLSKVRRE RMGHIELASP TAHIWFLKSL
     PSRIGLMLDM TLRDIERVLY FESFVVTEPG MTTLERGQLL TDEEYFDAME EFGDEFEAKM
     GAEAVQQLLM ELDLVEEIKI LREEVESTNS DTKLKKLSKR LKLMEAFKDS GNAPEWMVLT
     VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLSAPDI IVRNEKRMLQ
     ESVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVIVVGPT
     LKLHECGLPK KMALELFKPF IFAKLEGRGL ATTIKAAKKM VERETAEVWD ILAEVIREHP
     VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLTLEAQLEA
     RALMMSTNNI LSPANGEPII GPTQDVVLGL YYISRDRVNA QGEGHVFADT KEVMRALGNK
     QVHIHARVKV RVHEVVKDLE GNVEERTFIA DTTPGRCKLW DIVPAGLGFD MVNQNMTKKA
     ISKLLNTCYR ILGTKETCIF ADQLMYLGFR EATLSGSSIG VEDMVIPDAK YTMIDAAEEE
     VREIEEQFAS GLVTRGERYN KVVDIWARTN DQIAKAMMEN LRVEVVKNRD GKDEEQGSFN
     SIFMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIT SNFREGLNVL QYFISTHGAR
     KGLADTALKT ANSGYLTRRL VDVAQDLVVN HIDCGTEEGL LMTPLIEGGD VVEPLRERVL
     GRVVARDVMN PLNQDEVAVE AGTLLDEVWV AQLETMGVDE VLVRSPITCA TRWGVCATCY
     GRDLARGHQV NVGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRASAVSS IQIKHGGKVR
     FHNAKHVQHK DGLVIVSRSA DLAVADELGR ERERYKLPYG ATVTVNEGDE VSGGQVVATW
     DPHTHPIIAE VEGKVQFGDM EEGITVNHQT DELTGLTNIE MLSSQNRPSA GKDMRPVIRV
     LDSKGKPIVM PNTDMPAQYF LPGGALCGLK DGANIGVGDV IARIPQESSK TRDITGGLPR
     VADLFEARNP KEAAILAEKT GTVSFGKETK GKVRLVITPD NSDDNYEELI PKWRQLNVFE
     GERVEKGEVV SDGPLNPHDI LRLKGESELA RYIVNEVQEV YRLQGVKIND KHIETIIRQM
     LRKVEILEVG ESHFIKGEQA EYARVMEEID RLKAEDKMLP QYQRLLLGIT KASLATESFI
     SAASFQETTR VLTEAAVTGK EDDLRGLKEN VVVGRLIPAG TGYAYHMERR RQRADARGPE
     APTMDEVEAA LSEALSSSGE
 
 
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