RPOC_SALRD
ID RPOC_SALRD Reviewed; 1448 AA.
AC Q2S1Q6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=SRU_1757;
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=309807;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31;
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC43640.1; -; Genomic_DNA.
DR RefSeq; WP_011404501.1; NC_007677.1.
DR RefSeq; YP_445875.1; NC_007677.1.
DR AlphaFoldDB; Q2S1Q6; -.
DR SMR; Q2S1Q6; -.
DR STRING; 309807.SRU_1757; -.
DR PRIDE; Q2S1Q6; -.
DR EnsemblBacteria; ABC43640; ABC43640; SRU_1757.
DR GeneID; 61496385; -.
DR KEGG; sru:SRU_1757; -.
DR PATRIC; fig|309807.25.peg.1824; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000008674; 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 InterPro; IPR011054; Rudment_hybrid_motif.
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 SUPFAM; SSF51246; SSF51246; 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..1448
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240823"
FT REGION 1408..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
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 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 1448 AA; 161773 MW; CB8398269B91E81F CRC64;
MPYGNSKEIE TDFDSITISL ASPEDILERS YGEVMKPETI NYRSFKPEMG GLFCEKIFGP
VKDYECHCGK YKRIRYKGII CDRCGVEVTR KAVRRERMGH ISLSVPVVHI WYFKTLPNKI
GHLLGLKSKD LEKVIYYENY IVIQPGTAER LGVEENQLLT EEEYYEILYQ IRDDNNRLQD
DNEEKFIAKI GGEAVETMLE RLELDKLAQE LRYQVRTETS QQRKSKALKR LDVVEAFREA
NEDGTNKPEW MVMRVIPVIP PELRPLVPLD GGRFATSDLN DLYRRVIIRN NRLKRLIDIK
APEVILRNEK RMLQEAVDSL FDNSRKSNSV RGSSNRPLKS LSDMLKGKQG RFRQNLLGKR
VDYSGRSVIV SGPHLELHQC GLPKEMAVEL FKPFIIRRLI ERGIVKTVKS AKKYVDKKTE
DVWDILEKVI QGRPVLLNRA PTLHRLGIQA FQPVLTENKA IEIHPLVCPA YNADFDGDQM
AVHVPLSHEA CLESMVLMLS SHNVRSPADG GPLAVPSQDM ILGLYYITKA KSNQKGEGMR
FANVQEVRQA FDQDQVALHA KIQLRDPDGS GEMIDTTVGR VIFNETLPDT LDYVNEVLST
KNVRPVIARV LKQTGFEETA DFLDAIKDMG FRRSTTSGMT FSLSDIIIPD EKEELIEEAN
ETVEEAEQNY SMGFITDNER YNQVIDVWTK TNNKVSEVLF DALKEHKEGF NPIFTMADSG
ARGSQEQIRQ LGGMRGLMAK PQKNIGEGGG GGEILENPIL SNFKEGLTVQ EYFISTHGSR
KGLADTALKT ADAGYLTRRL VDVSQSVTVT EHDCGTLRGI NVGALKDNEE VVAPLSDRIT
GRVSVRDVYD PHTDELIVEA NELITDEIAD DIAQTSIEEI EIRSVLTCEA ERGVCTLCYG
QNLATGRMVE VGESVGVVAA QSIGEPGTQL TLRTFHTGGT ATREVGESTI QAKFAGTLEF
ENLRTVTYED TDGPKEVVLS RQGEVRIMDT DGDRRELTSY VVPYGAELLV DEGEDVEDGD
VLASWDPYNS LILTEANGTV RFEDIIEDTT YREETDEQTG HKEKVIVESR ERTLTPAVIV
ETEDGEQREY NMPVDARIQV DEGDEVQAGQ TLAKMPRQAA QTSDITGGLP RVEELFEART
PDEPAVVSEI DGIVSFGDQK RGSQEVIVTS RDGDMEKSYM VSLSKHMLVH EGDYVEAGDR
LCDGQIAPHD ILSIKGPRAV QEHLLNEVQE VYRLQGVDID DKHFEVVIRQ MMKRVKITEP
GDTNFLEEDQ VDRQKMASIN DDLYDKFVVK DPSDANVEIG EVIGRRRLRE LNSELKREDK
PEIEVREARP AVGEPLLLGI TKASLATDSM ISAASFQETT KVLTNSAIRS RTDPLEGLKE
NVVAGHSIPA GTGQREYRDL VVGSKSELEE LQAAIGGDGE SPSGDGAAGD GAPSEEDVEQ
IEASGSEN
