ID L0RVZ2_MYCC1 Unreviewed; 1496 AA.
AC L0RVZ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN Name=MCYN0585 {ECO:0000313|EMBL:CCP24317.1};
GN Synonyms=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN OrderedLocusNames=MCYN_0585 {ECO:0000313|EMBL:CCP24317.1};
OS Mycoplasmopsis cynos (strain C142) (Mycoplasma cynos).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=1246955 {ECO:0000313|EMBL:CCP24317.1, ECO:0000313|Proteomes:UP000010466};
RN [1] {ECO:0000313|Proteomes:UP000010466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C142 {ECO:0000313|Proteomes:UP000010466};
RX PubMed=23409256; DOI=10.1128/genomeA.00196-12;
RA Walker C.A., Mannering S.A., Shields S., Blake D.P., Brownlie J.;
RT "Complete genome sequence of Mycoplasma cynos strain C142.";
RL Genome Announc. 1:E00196-E00196(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|HAMAP-Rule:MF_01322,
CC ECO:0000256|RuleBase:RU004279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01322}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HF559394; CCP24317.1; -; Genomic_DNA.
DR STRING; 1246955.MCYN_0585; -.
DR KEGG; mcy:MCYN_0585; -.
DR PATRIC; fig|1246955.3.peg.528; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR Proteomes; UP000010466; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
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; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 2.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01322};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000010466};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01322};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01322}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT DOMAIN 329..610
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT REGION 406..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 556
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 558
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 560
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 1136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1496 AA; 169895 MW; BEE95BD4126D28BF CRC64;
MKKKMIIKYC NLNQEVKVNN SNSNAHKERI KRITLSLATR EDVKNWSHGE VTKPETINYK
TYKPEKDGLF DELIFGPVID YKCPICGSKY KKSDVNEVCG KLPQCKKYNP EILPKITRRS
RMGHITLHNP VVHFWFFKID HSVISNLLGL RVERGNEKQN VTKSDLEKLI YYKSHIVLES
GNLKSLNKNT IIDINEAANI YDKALEELLE IYKDDKEAYE IISESLWELR EYAKSQDGKD
FGIDFYQYNE VINEYSDAKI GTGSAAIEYL LSNIDLEKEQ KLVQEQIDKI NAEINKQRDV
STSKIQARQK LYKRLTIISS FIRSGQKPTD MLIYELPVIP ADLRPLVQLD GGRHSTSDIN
ELYRRIIIRN NRLAKWNETD APMLIKQNEY RMIQEAVDSL IDNARKKPTP VSSRDNHPLK
SISDGLTGKK GRFRQNLLGK RVDYSARSVI VGGPSLKMYE VGVPRDIAAK LFEPWIIKEL
IAHEEGITSI KTAKKLIENL DPRIWPYVEK AIQGRPVLLN RAPTLHRLSI QAFQPVLIRA
KAIKLHPLVT TAFNADFDGD QMAIHVPISE KAVREAQELM LASKNILGPK DGEPIINPSQ
DIILGLYYLT IEKSGENAKG EGNFYSNIDE MLLAYERGHV SLHSRVVLPI KSLNKPKLQL
QTTKPYIFST VGKFLLNSVL PTEFEFVFGK YVEKTYKKSL NNEMQLVERE VIHTSKNDLD
HYTFDYGTNF YETFKNIDLN LALSKKDIAR IIRKIYEEYV AVITIEDIAS ILNKINKFNF
KEQLEACEDL VDYKGEKIPS THAKLINQFI IDEFEKISYS YKVNEAQKDS SDWNVHEYTK
GLENVWFKYS NYVSYILDKI KDLGFKYSTI SGTTISMNDV KTLDSTADFI KEGEEYIKEL
KAFFEYGYLT DDERYKLTIE KWSKVKEKIE KSLKEVTKLD IDNPLFMMMT SGARGNASNF
TQLAGMRGLM SNNTKVLKAD AENDRVVRST IEIPVKSSFL DGLSSYEFYS STHGARKGLT
DTALNTAKSG YLTRRLVDVA QSIVVREADC GSDFGFVVKA IKDTKTDTII ETLYERIEGR
YTNKAIYDHS GNLVIDANEL ITPEIANIIV NDLKLAEVEI RSVLSCHTKN GVCKICYGKD
LASNRVVNIG EAVGIVAAQS IGEPGTQLTM RTFHTGGVAG VEDITGGFGR LIELIDAYDN
PWGKPAEISK VYGIISNIEQ VTNKETGKVT DFIEVSITTK NEQGDEIIET ISGRSSQKLR
VKVGDHVVPG QKIFEGPIVL NQLLNATDAR TVQSYLLKEI QRLYRLQGIT IADKYIEIII
SQMLSKILII EPGDSRFFSG ALVDTYVYQV ENSKLLSAGK KPAYGKVKIS GAKQIPLLSN
SFLSAASFQE TAKILVNSSV AQRVDYLEGL KENIILGQKI PAGTNSDYEL KGKYDIRSFK
SYFPDKFDPD LNSEEPITNF LDENFSINDI TDEAYHNDIF DQSDEFTNYY DFEDDM
//
