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RPOC_ACIBT
ID   RPOC_ACIBT              Reviewed;        1397 AA.
AC   A3M1G4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
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=A1S_0288;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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; CP000521; ABO10758.2; -; Genomic_DNA.
DR   RefSeq; WP_000653927.1; NZ_CP053098.1.
DR   AlphaFoldDB; A3M1G4; -.
DR   SMR; A3M1G4; -.
DR   GeneID; 66398728; -.
DR   KEGG; acb:A1S_0288; -.
DR   HOGENOM; CLU_000524_3_1_6; -.
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; Transcription; Transferase; Zinc.
FT   CHAIN           1..1397
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000308816"
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         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         467
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         819
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         893
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"
FT   BINDING         903
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1397 AA;  155051 MW;  197429826058DA14 CRC64;
     MKDLLDIMRK KTDSDGHAPV EFDRIRIGLA SPEMIKSWSH GEVKKPETIN YRTFKPERDG
     LFCAKIFGPV KDYECLCGKY KRMKYKGVIC EKCGVEVTTA KVRRERMGHI ELASPVAHIW
     FLKSLPSRIG LLLDMTLRDI ERVLYFESYV VTDPGMTPFE KYQLLNDEEY FTALEEHGDE
     FVAKMGAEAV QDLLKDIDLE AEISRLREEI PQTTSETKLK KASKRLKLME AFKDSNNKPE
     WMVMNVLPVL PPDLRPLVPL EGGRFATSDL NDLYRRVINR NNRLKRLLDL AAPDIIVRNE
     KRMLQESVDA LLDNGRRGRA ITGSNKRPLK SLADMIKGKQ GRFRQNLLGK RVDYSGRSVI
     TVGPTLRLHQ CGLPKKMALE LFKPFIFAKL QASGQATTIK AAKKMVERET PEVWDVLASV
     IRQHPVMLNR APTLHRLGLQ AFEPILIEGK AIRLHPLVCA AFNADFDGDQ MAVHVPLTLE
     AQLEARALMM STNNILSPAN GEPIIVPSQD VVLGLYYITR DAVNAKGEGM VFADTHEVNR
     ALATGQVAIH ARVKVRVHQT VINENGEREQ QTIIVDTTPG RCLLWEVVPE GLSFDMINLE
     MTKKNISKLI NSCYRKLGLK DTVIFADQLM YLGFRQATRS GVSVGMEDML IPPTKHTIID
     KAETEVREIE QQFEQGFVTA GERYNKVVDI WARTNDQVAK AMMDNLSYTL VKNKQGEDEK
     QKSFNSIYMM SDSGARGSAA QIRQLAGMRG LMAKPDGSII ETPIKANFRE GLTVLQYFIS
     THGARKGLAD TALKTANSGY LTRRLVDVAQ DLVITEPDCG TSGGLVMTPF IQGGDVIEPL
     RDRVLGRVTA EDVRRASDDE VVLPRGTLID EKIAAQLEEA GVDEVKVRSV IACESTFGVC
     AKCYGRDLAR GHLVNPGESV GVMAAQSIGE PGTQLTMRTF HVGGAASRTS AANSVQVRNK
     GTVRFHNVKT VQHAKGHLVS VSRSGEIGIA DELGRERERY KLPYGASILL KDGELVEAGG
     IVATWDPHTH PLVTEVAGKA RFSQIADGVT ATSKTDDATG MTTVEILPVT ARPASGKDLR
     PAIVLDTTDG GEQFYFLPQN TIVTVRDGET IGVGDVIGRV PQESSRTRDI TGGLPRVADL
     FEARKPKEHA ILAEVSGIVS FGKETKGKNR LVITPDDGSE IYEELIPKWR QINVFEGEHV
     NRGETISDGP QNPHDILRLK GEVALTNYIV NEVQDVYRLQ GVKINDKHIE VIVRQMLRKV
     DIIDGGDTSF IKGEQVDYIR VVQENQAVLA QNKFPAKFER QLMGITKASL STDSFISAAS
     FQETTRVLTE AAVTGKEDDL RGLKENVVVG RLIPAGTGLA YHLERRRQEA EAAEHALHND
     FSEVDQAFSQ ALNSEQF
 
 
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