RPOC_AMOA5
ID RPOC_AMOA5 Reviewed; 1433 AA.
AC B3ETY9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Aasi_1395;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE06691.1; -; Genomic_DNA.
DR RefSeq; WP_012473433.1; NC_010830.1.
DR AlphaFoldDB; B3ETY9; -.
DR SMR; B3ETY9; -.
DR STRING; 452471.Aasi_1395; -.
DR PRIDE; B3ETY9; -.
DR EnsemblBacteria; ACE06691; ACE06691; Aasi_1395.
DR KEGG; aas:Aasi_1395; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001227; 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 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..1433
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141757"
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 823
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 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1433 AA; 160565 MW; 3C6E27BFAA19FAF6 CRC64;
MLARKDTRVK SDFSEIIISL ASPESILERS RGEVTQPETI NYRTYKPEMK GLFCERIFGP
VKDWECHCGK YKRIRYKGII CDRCGVEVTE KKVRRERTGH IELVIPVAHT WYFRSLPSKI
GNLLGFPTKK LDQIIYYERY VVVQPGIKAE EGLSYMDFLT EEEYLDILDS LPRENQLLDD
SDPKKFIAKM GAEALEFMLS RIDLDTLSSE LREQAHTDTS QQRRIEALKR LKIVEAFRDA
KTRIANRPEW MVMRIIPVIP PELRPLVPLD GGKFATSDLN DLYRRVIIRN NRLKRLIDIK
APEVILRNEK RMLQEAVDSL FDNSRKVNTV VAEGSRVLKS FSDILKGKQG RFRQNLLGKR
VDYSGRSVIV VGPELKLHEC GLPKDMAAEL FKPFIIRRLI ERGIVKTVKS AKKLVEKKTP
VVWDILENVL KGHPILLNRA PTLHRLSIQA FQPKLIEGKA IQLHPLVCAA FNADFDGDQM
AVHVPLSHEA IAEASLIMLA SHNILNSANG TPLAVPTKDM ILGLYYLTKG RKSTPEHPVK
GEGMTFFSAQ EVIIGIDTGQ VSIHALVKVK IKDKDEQGET IEHIVDTIAG RVVFNQYVPE
ELGFINELLT SKKLQHITSQ VYRLVGTSRA TQFLDDVKSL GFRNAYKAGV SFALDDIKVP
TIKFELIEQA QREVNAVQEN YLMGLITDNE RYNQIIDIWT RVNTQVTVFL MQELEEDRQG
FNSIFMMMNS GARGSREQVR QLGGMRGLMG KPQKQLQGSV GEIIENPILS NFKEGLDVLE
YFISTHGARK GLADTALKTA DAGYLTRRLV DVAQDVITTE EDCGTLRGVT ITTSINKDEV
AESISERTLG RISLNDIYDP VTNNLLVNAG EEITEEIAAY IESVGIESIE VRSVLTCETR
RGICTKCYGR NLSTGKLVQI GEAVGVIAAQ SIGEPGTQLT LRTFHVGGAA SSIGVESNIQ
ATDKGVLQFE DFNTIKTTNP QGEQLDVIIS RSCEVRLLNP QDNRILMHKH VPYGAYLRVK
QGELIEKGQE ICYWDPYNAV ILTSIDGEIE FHSIEEGITY KEEYDEQTGY KEKVIIESKD
KTKNPSITVK GSSGEAINYN IPVKARLIVE DGTKIKAGHP LVKIPRVVSL SKDITGGLPR
VTELFEARDP SNPSIVSEID GFVTYGPIKR GSREIFVESK DGIRRKYLVP LSKHILVQDN
DYIKAGYPIS DGNTSPSSIL HIKGPIAVQE YIAKELQAVY RLQGVKINDK HIEVIIRQML
SKLEVIESGD TTFLPGQTVS KFTFREGNDQ LLDKKVVIDA GSSSVLRVGQ IITARALHEE
NSNLKRDKLS LVQARDAQPA IARLKLQGIT QASLDTKSFI SAASFQDTTR VLSEAAIRGK
RDRLQGLKEN VIVGHLIPTG TGLPRYSKMI IGLREDYENL VASREKQAAT DNI
