GREA_MYCTU
ID GREA_MYCTU Reviewed; 164 AA.
AC P9WMT9; L0T5S2; O53428; P64279;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Transcription elongation factor GreA {ECO:0000255|HAMAP-Rule:MF_00105};
DE AltName: Full=Transcript cleavage factor GreA {ECO:0000255|HAMAP-Rule:MF_00105};
GN Name=greA {ECO:0000255|HAMAP-Rule:MF_00105}; OrderedLocusNames=Rv1080c;
GN ORFNames=MTV017.33c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, DETERMINATION OF TRANSLATIONAL START
RP SITE, AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17259624; DOI=10.1099/mic.0.2006/001537-0;
RA Rison S.C., Mattow J., Jungblut P.R., Stoker N.G.;
RT "Experimental determination of translational starts using peptide mass
RT mapping and tandem mass spectrometry within the proteome of Mycobacterium
RT tuberculosis.";
RL Microbiology 153:521-528(2007).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Necessary for efficient RNA polymerase transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by cleavage factors such
CC as GreA or GreB allows the resumption of elongation from the new
CC 3'terminus. GreA releases sequences of 2 to 3 nucleotides.
CC {ECO:0000255|HAMAP-Rule:MF_00105}.
CC -!- SIMILARITY: Belongs to the GreA/GreB family. {ECO:0000255|HAMAP-
CC Rule:MF_00105}.
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DR EMBL; AL123456; CCP43831.1; -; Genomic_DNA.
DR PIR; F70894; F70894.
DR RefSeq; NP_215596.1; NC_000962.3.
DR RefSeq; WP_003405742.1; NZ_NVQJ01000080.1.
DR AlphaFoldDB; P9WMT9; -.
DR SMR; P9WMT9; -.
DR STRING; 83332.Rv1080c; -.
DR iPTMnet; P9WMT9; -.
DR PaxDb; P9WMT9; -.
DR DNASU; 887115; -.
DR GeneID; 45425053; -.
DR GeneID; 887115; -.
DR KEGG; mtu:Rv1080c; -.
DR TubercuList; Rv1080c; -.
DR eggNOG; COG0782; Bacteria.
DR OMA; TWLTQEA; -.
DR PhylomeDB; P9WMT9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070063; F:RNA polymerase binding; IEA:InterPro.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
DR Gene3D; 1.10.287.180; -; 1.
DR Gene3D; 3.10.50.30; -; 1.
DR HAMAP; MF_00105; GreA_GreB; 1.
DR InterPro; IPR036953; GreA/GreB_C_sf.
DR InterPro; IPR018151; TF_GreA/GreB_CS.
DR InterPro; IPR006359; Tscrpt_elong_fac_GreA.
DR InterPro; IPR028624; Tscrpt_elong_fac_GreA/B.
DR InterPro; IPR001437; Tscrpt_elong_fac_GreA/B_C.
DR InterPro; IPR023459; Tscrpt_elong_fac_GreA/B_fam.
DR InterPro; IPR022691; Tscrpt_elong_fac_GreA/B_N.
DR InterPro; IPR036805; Tscrpt_elong_fac_GreA/B_N_sf.
DR PANTHER; PTHR30437; PTHR30437; 1.
DR Pfam; PF01272; GreA_GreB; 1.
DR Pfam; PF03449; GreA_GreB_N; 1.
DR PIRSF; PIRSF006092; GreA_GreB; 1.
DR SUPFAM; SSF46557; SSF46557; 1.
DR TIGRFAMs; TIGR01462; greA; 1.
DR PROSITE; PS00829; GREAB_1; 1.
DR PROSITE; PS00830; GREAB_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17259624,
FT ECO:0007744|PubMed:21969609"
FT CHAIN 2..164
FT /note="Transcription elongation factor GreA"
FT /id="PRO_0000176943"
FT COILED 50..76
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00105"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 164 AA; 17855 MW; 22C65042E6DF3529 CRC64;
MTDTQVTWLT QESHDRLKAE LDQLIANRPV IAAEINDRRE EGDLRENGGY HAAREEQGQQ
EARIRQLQDL LSNAKVGEAP KQSGVALPGS VVKVYYNGDK SDSETFLIAT RQEGVSDGKL
EVYSPNSPLG GALIDAKVGE TRSYTVPNGS TVSVTLVSAE PYHS
