RPOC_SHEPW
ID RPOC_SHEPW Reviewed; 1404 AA.
AC B8CNC6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=swp_2004;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ28760.1; -; Genomic_DNA.
DR RefSeq; WP_020912133.1; NC_011566.1.
DR AlphaFoldDB; B8CNC6; -.
DR SMR; B8CNC6; -.
DR STRING; 225849.swp_2004; -.
DR PRIDE; B8CNC6; -.
DR EnsemblBacteria; ACJ28760; ACJ28760; swp_2004.
DR KEGG; swp:swp_2004; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000753; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1404
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141792"
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 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1404 AA; 155072 MW; 5781B3F930ED0E25 CRC64;
MKDLLKFLKQ QSKTEEFEGI KIGLASPDLI RSWSFGEVKK PETINYRTFK PEREGLFCAR
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIDLASP VAHIWFLKSL
PSRIGLMLDM TLRDIERVLY FESFVVIEPG MTSLERGQML TEENYLDALE EYGDEFEAKM
GAEAVLELLR AIELEKEIEM MREELPSINS ETRRKKITKR LKLIEAFFQS GNKPEWMILK
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ
ESVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVITVGPT
LRLHQCGLPK KMALELFKPF IYGKLEGRGL ATTIKAAKKM VEREVPEVWD VLDDVIREHP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA
RSLMMSTNNI LSPANGEPVI TPSQDVVLGL YYTSRECVNG KGEGMAFESV AEAEKAYRTG
AAELHARVKV RITETKTDEA GEKVKTRRIV DTTVGRALLS LILPKGLSFD LVNQNMGKKQ
ISKLLNTCYR QLGLKDTVIF ADQLMYTGFH FATVSGASVG INDMVIPDEK YTLVADAEAE
VLEIQEQFQS GLVTAGERYN KVIDIWASAN EKVSKAMMDN LSSETVINRD GEEEKQESFN
SIYMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLNVS QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVAQDLVVI EEDCGTFEGL TMKPLIEGGD VVEPLRERVL
GRVVAQDVFK PGTEEVLIPR NTLLDEAWCD TVEDNSIDEM IVRSVISCDT DFGVCAACYG
RDLARGHIIN QGEAIGVVAA QSIGEPGTQL TMRTFHIGGA ASRASAENNV QVKNAGTLKL
HNAKHVTNSE GKLVIVSRSS ELAIIDELGR EKERYKVPYG TVLEKLEDAP VAAGEIIANW
DPHTHPIITE VAGSTKFVDM IEGVTMTRQT DELTGLSSIV VLDVAQRPTA GKEMRPMIRL
VAADGGDLMI PGTEVPAQYF LPGNAIVNLD DNAPINVGDA LARIPQESSK TRDITGGLPR
VADLFEARKP KEPAILAEVS GTISFGKETK GKRRLVITPA EGGDHYEEMI PKWRNLNVFE
GEKVERGEVI ADGPEAAHDI LRLRGIHNVA NYIVNEVQDV YRLQGVKIND KHIEVIIRQM
LRKCEIANAG DSEFLAGEQA EVSRVKIANR ELEAQGKQPA TFERELLGIT KASLATESFI
SAASFQETTR VLTEAAVGGK SDKLRGLKEN VIVGRLIPAG TGYSYHQKRA EAAVKPAAEE
APAISASEAE QNLADLLNLA GSSD
