RPO12_HALLT
ID RPO12_HALLT Reviewed; 44 AA.
AC B9LTN3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo12 {ECO:0000255|HAMAP-Rule:MF_00615};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00615};
DE AltName: Full=DNA-directed RNA polymerase subunit P {ECO:0000255|HAMAP-Rule:MF_00615};
GN Name=rpo12 {ECO:0000255|HAMAP-Rule:MF_00615};
GN Synonyms=rpoP {ECO:0000255|HAMAP-Rule:MF_00615};
GN OrderedLocusNames=Hlac_0565;
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_00615}.
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_00615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00615};
CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00615};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00615}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00615}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA
CC polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00615}.
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DR EMBL; CP001365; ACM56167.1; -; Genomic_DNA.
DR RefSeq; WP_004049526.1; NC_012029.1.
DR AlphaFoldDB; B9LTN3; -.
DR SMR; B9LTN3; -.
DR STRING; 416348.Hlac_0565; -.
DR EnsemblBacteria; ACM56167; ACM56167; Hlac_0565.
DR GeneID; 7401700; -.
DR KEGG; hla:Hlac_0565; -.
DR eggNOG; arCOG04341; Archaea.
DR HOGENOM; CLU_179456_2_1_2; -.
DR Proteomes; UP000000740; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; 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 HAMAP; MF_00615; RNApol_arch_Rpo12; 1.
DR InterPro; IPR006591; RNAP_P/RPABC4.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR023464; Rpo12.
DR Pfam; PF03604; DNA_RNApol_7kD; 1.
DR SMART; SM00659; RPOLCX; 1.
DR SUPFAM; SSF63393; SSF63393; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..44
FT /note="DNA-directed RNA polymerase subunit Rpo12"
FT /id="PRO_1000194780"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
SQ SEQUENCE 44 AA; 5050 MW; D6140DCAA4CADFBC CRC64;
MSYKCSRCKR DVTLDEYGGV RCPYCGHRVL LKERGGDVKE VNVE
