ID B6XVC6_9BIFI Unreviewed; 1246 AA.
AC B6XVC6;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 ECO:0000313|EMBL:EEB21327.1};
GN ORFNames=BIFCAT_01156 {ECO:0000313|EMBL:EEB21327.1};
OS Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=566552 {ECO:0000313|EMBL:EEB21327.1, ECO:0000313|Proteomes:UP000003882};
RN [1] {ECO:0000313|EMBL:EEB21327.1, ECO:0000313|Proteomes:UP000003882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB21327.1,
RC ECO:0000313|Proteomes:UP000003882};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB21327.1, ECO:0000313|Proteomes:UP000003882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB21327.1,
RC ECO:0000313|Proteomes:UP000003882};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EEB21327.1}.
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; ABXY01000016; EEB21327.1; -; Genomic_DNA.
DR AlphaFoldDB; B6XVC6; -.
DR eggNOG; COG0086; Bacteria.
DR Proteomes; UP000003882; 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; -; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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};
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 220..499
FT /note="RNA polymerase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00663"
FT COILED 61..96
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 804
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT BINDING 883
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 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1246 AA; 137619 MW; 8F87F87F8E7541CA CRC64;
MGHIELAAPV THIWFFKGVP SRLGYLLDIA PKDLEKVIYF AAYMVTSVDE EQRHEDLPGL
QDEFDNDIAN LEKRRNAEIE ERAKKVESDL AELEAEGEAR GSARAKLRNS AEREMAAIRI
RFDEQIQRLS AVFDRFKNLK PGDMEGDVDL WREMEDRYGD YFEGCMGAEA IKKRLQDFDL
EAASKQLREE IDTGTGQRKA RALKRLKVVN AFLTTGNKPE AMVLDVIPVI PPDLRPMVQL
DGGRFATSDL NDLYRRVINR NNRLKRLIEL GAPEIMLNNE KRMLQEAVDS LFDNGRRGRP
VTGASNRPLK SLSDMLKGKQ GRFRQNLLGK RVDYSGRSVI VVGPSLRMHQ CGLPKPMALE
LFKPFVIKRL VDLNYAQNMK SAKRLVDRGD SEVWGVLEEV IAEHPVLLNR APTLHRLGIQ
AFEPILVEGK AIHLPPLACA AFNADFDGDQ MAVHLPLSAE AQAEARSLMM ASDNILKPAD
GHTVTMPSQD MILGLYYLTT VIDGAKGQGR VFSSLEEAEM ALDKHEIDMQ AKVLIRLPED
FVLPKGWEPS EIEVVDPEPG SPAVVKEERF HDGSVLFATS YGRILFNSTL PVDYPFVNDQ
APKKRLSKIV DDIATRYSTA QVAATLDALK DMGFTRAPWS GVSFAFSDVI QPSERDEFIE
KYEAEAEKVN ENYEIGMLTE EERRQELIDL WTKCTSEVSE AVEEHFDSKN NLAIIVQSGA
RGNMMQINQI AGMRGLVANP KGEIIPRPVK SNYRDGLSVL EYFISQHGAR KGLADTALRT
AESGYLTRRL VDVSQDVIVR EEDCGTKRGL TMKVGERDAE GNLHLVKAAD GGPYSRLLAA
DVIDPADGET VLYKAGDALS MDVLNDLVAH DVEEVKARSV LTCDSKRGVC AKCYGWSLAT
NKLVDVGEAV GIVAAQSIGE PGTQLTLRSF HSGGVASASD ITQGLPRVTE LFEARTPKGE
APIAEFAGVV KVEDTERGRQ VMLKPDDESV EPIVYPVTRR APMLVKDGEH VEAGTQLIEG
SVDPKKILRI LGPRAAQVNI VEEVHTVYRS QGVDIHDKHI EVIVHQMLRR ITVIDSGDTD
LLPGELVDQA RFKASNMKAV KEGGKPAAGR PELMGITKAS LATDSWLSAA SFQETTRVLT
EAALSQKVDD LKGLKENVII GKLIPAGTGL ARYRNAVVEP DKAIRDTIYP NFGLGGDESD
AAFGDADLSE VDFSNIDFGD LKLGDDFNPD DFLDDNGGQM DLGDNL
//
