RPOC_AKKM8
ID RPOC_AKKM8 Reviewed; 1398 AA.
AC B2UQY1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Amuc_1040;
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC 107961 / Muc;
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
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; CP001071; ACD04866.1; -; Genomic_DNA.
DR RefSeq; WP_012420081.1; NC_010655.1.
DR AlphaFoldDB; B2UQY1; -.
DR SMR; B2UQY1; -.
DR STRING; 349741.Amuc_1040; -.
DR PRIDE; B2UQY1; -.
DR EnsemblBacteria; ACD04866; ACD04866; Amuc_1040.
DR GeneID; 60880508; -.
DR KEGG; amu:Amuc_1040; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; AMUC349741:G1GBX-1111-MON; -.
DR Proteomes; UP000001031; 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; -; 1.
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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1398
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353282"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
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 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1398 AA; 155528 MW; 59E8BBFC3746A49C CRC64;
MSDTPTIREM HGLSDKPRTF DQVAITVADP DTIRSWSFGE VVNPETINYR TFKPEKGGLF
CERIFGPTRD MECACGKYKR IKHKGITCDR CGVEVTNARV RRERMGHIEL AVPVSHIWFY
KCMPSRIGLM LDMTARHLER VIYYEDYIVV DPGSTPLEKG AILTEEEFRN AEDEYGYDSF
EAGMGAEAIQ KMLAAIDLPT LVADLQEQLD NTNSKQNKRK IAKRLKLAQG FLQSNTRPEW
MILNVLPVIP PDLRPLVPLE GGRFATSDLN DLYRRVINRN NRLKTLLSLK TPEVIIRNEK
RMLQEAVDAL FDNGRHGRAV TGAGNRPLKS LSDMLKGKGG RFRQNLLGKR VDYSGRSVIV
IGPELKLNQC GLPKKMALIL FEPFIIHRLK ELGYVHTVRS AKKLIDRKTP EVWDILEEVT
KGHPVMLNRA PTLHRLSIQA FEPVLIEGSA IRLHPLVCNA YNADFDGDQM AVHVPLSVEA
QMEARQLMLA PNNIFSPASG KPIATPTQDI ILGAYFLTHT RAAEVQNNQD NHHHLPLFES
IDEVEYAIAA RKIGYHDWIR LHNPDYGKKP SEVVYGDVTK KVIITTAGRV RFNEIWPREL
GYINRNVGKK QMGDIIWRCY QTVGKERTVQ TLDALKNLGF KEATRSGCSI GIVDMVVPSQ
KKTEIEKAYA ELDKVTRQYK NGIITDGERY QKVVDIWTQT TDVIQAALYR KLEHNEGSKM
ASPLFMMVDS GARGNKAQIK QLSGMRGLMA KPSGEIIERP ITANFREGLS VLEYFISTHG
ARKGLADTAL KTADSGYMTR KLVDVAQDVI VHAEDCGTSN GITVHAIYDG DEEVASLSSR
IYGRTSCERI VDPVSGEVIV DINDLINEKQ AEQLEKIGIE RLKIRSVLTC ELKKGCCAKC
YGLNLATGQE VKIGEAVGII AAQSIGEPGT QLTMRTFHVG GTATTAFKQP IVKAKNDGRV
IYTEDLRTVE NADGNFVVLN KNCSVRIENE QGRELESYQP VIGTILYVPN GGTIKKDETL
ATWDPYNVPV IAEKGGIVEF KDMIVGITVS KETDRETGAS SLVVMEHKQE LHPQVVIRDA
KTREVLAHHA IPAGANLTVK DGETISAGTM VAKTPRKVAK TKDITGGLPR VAELFEARKP
KDACTIARVE GIVRLSSKNT SRGKKVITIE TPTGELVDHL VPMNKHVIVH EDDHVHLGDQ
LTEGPVSPEE ILDVCGKERL QEHLVNEVQE VYRLQGVEIN DKHVEIIVRQ MLRKVVITEP
GNTEFLWGDQ VDKTTFDRIN EQTVAQGGQP AAAKPVLLGI TKASLETESF ISAASFQDTT
RVLTEASTLG KTDTLEGFKE NVIMGHLIPA GTGFSRYSKI EVEPAEGAEE IAAASEEEEA
AELAEDMLND TINFDNER
