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Database: UniProt
Entry: A0A066UMD7_9GAMM
LinkDB: A0A066UMD7_9GAMM
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ID   A0A066UMD7_9GAMM        Unreviewed;      1410 AA.
AC   A0A066UMD7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN   ORFNames=MBO_04097 {ECO:0000313|EMBL:KDN25378.1};
OS   Moraxella bovoculi 237.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN25378.1, ECO:0000313|Proteomes:UP000035860};
RN   [1] {ECO:0000313|EMBL:KDN25378.1, ECO:0000313|Proteomes:UP000035860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=237 {ECO:0000313|EMBL:KDN25378.1,
RC   ECO:0000313|Proteomes:UP000035860};
RX   PubMed=24970830;
RA   Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA   Reilly T.J.;
RT   "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT   Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL   Genome Announc. 2:e00612-14(2014).
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|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01322, 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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: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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN25378.1}.
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DR   EMBL; AOMT01000019; KDN25378.1; -; Genomic_DNA.
DR   RefSeq; WP_036364013.1; NZ_AOMT01000019.1.
DR   eggNOG; COG0086; Bacteria.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000035860; Unassembled WGS sequence.
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   CDD; cd01609; RNAP_beta'_N; 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; -; 3.
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   NCBIfam; TIGR02386; rpoC_TIGR; 1.
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; 1.
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:UP000035860};
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          237..516
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         817
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         890
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1410 AA;  155420 MW;  DAC810F8DF64B2D4 CRC64;
     MKDLLDIMKG PADNGIKEFD SIQISLASPD TIKSWSHGEV KKPETINYRT FKPERDGLFC
     AKIFGPVKDF ECLCGKYKRR KFQGIICEKC GVEVTAAKVR RDRMGHIELA SPVAHIWFLK
     SLPSRIGLLL DITLRDIERV LYFESYIVTD PGMTGLDKYQ LLDDEEYFNA LEQYGDEFIA
     KMGAEAVQDL LKDIDVDGEI DELRAEIPQT NSETKLKKMS KRLQLLESFR DSGNKPEWMV
     MTVLPVLPPD LRPLVPLEGG RFATSDLNDL YRRVINRNNR LKRLLELNAP DIIVRNEKRM
     LQEAVDALLD NGRRGRAITG SNKRPLKSLA DMIKGKQGRF RQNLLGKRVD YSGRSVIVVG
     PTLRLHQCGL PKKMALELFK PFTYAKLLQN NIAQTIKAAK KMVEREEPAV WDMLASVIRE
     HPVLLNRAPT LHRLGLQAFE PVLIEGKAIQ LHPLVCAAFN ADFDGDQMAV HVPLTLEAQL
     EARALMMSTN NILSPANGEP IIVPSQDVVL GLYYISRSHV NAKGENMVFS TVNEALRAIG
     SEDLSVNAKI KVRVTETILD EKTGEKTTKT EIKDTVAGRL LIWNIMPEGM AFSECNTEMT
     KKNISKLLNS CYRKLGVKES VLFADHLMYL GFAQATLSGI SIGMEDMVIP PTKKEIMDAA
     DSEVREIEQQ FEQGFVTAGE RYNKVVDIWS RTSDKIANAM MENLSTDEVV NADGEVEKEK
     SFNSIYMMAD SGARGSATQI RQLAGMRGLM AKPDGSIIET PIKANFREGL TVLQYFISTH
     GARKGLADTA LKTANSGYLT RRLVDVAQDL VITHDDCGTD AGQRMTPVID GGEIVERLGD
     RVLGRVTAKD VVNVDGEVTA PAGTLIDERM VEKLDANAID EVYVRSVITC ESSHGVCAKC
     YGRDLARGHL VNIGESVGVM AAQSIGEPGT QLTMRTFHVG GAASAAAVDN SVSVGSNGSV
     RFHNMKTVEH VDGHLVTVSR SAEIGVADSQ GRERERYKVP YGSNVLVRDG AEVSAGDVIA
     KWDPHTHPII TEFAGTARFS DITDGMTATV KVDETTGMSS FEILASKDRP SIAKDLRPAI
     ILDTTEGKEV VYFLPAETVI RVSEGETVTA GSVLGRVPQA TSGTKDITGG LPRVADLFEA
     RRPKDHAIMA EMSGVVSFGK ETKGKNRFII TDEEGNVHEE LIPKWRQINV FEGETVERGE
     VVSDGPQNPH DILRLKGETA LANYIVNEVQ EVYRLQGVKI NDKHIEVIVR QMLRKVEVTD
     GGDSSYFKGD QAEYTKIRAL NEELVANNKF PVQFERQLLG ITKASLATES FISAASFQET
     TRVLTAAATM GKVDDLTGLK ENVVVGRLIP AGTGLAYHQN RQRKAELALE GNASADDIAL
     DDELLTSSEN LPTEDSFAKA FADELGQDSE
//
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