SPT5_METJA
ID SPT5_METJA Reviewed; 147 AA.
AC Q57818;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Transcription elongation factor Spt5 {ECO:0000255|HAMAP-Rule:MF_00950};
GN Name=spt5 {ECO:0000255|HAMAP-Rule:MF_00950}; OrderedLocusNames=MJ0372;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 1-83, DOMAIN, AND SUBUNIT.
RX PubMed=19475703; DOI=10.1002/prot.22465;
RA Zhou H., Liu Q., Gao Y., Teng M., Niu L.;
RT "Crystal structure of NusG N-terminal (NGN) domain from Methanocaldococcus
RT jannaschii and its interaction with rpoE''.";
RL Proteins 76:787-793(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-82, FUNCTION, SUBUNIT, DOMAIN,
RP AND MUTAGENESIS OF ALA-4; TYR-42 AND LEU-44.
RX PubMed=20197319; DOI=10.1093/nar/gkq135;
RA Hirtreiter A., Damsma G.E., Cheung A.C., Klose D., Grohmann D., Vojnic E.,
RA Martin A.C., Cramer P., Werner F.;
RT "Spt4/5 stimulates transcription elongation through the RNA polymerase
RT clamp coiled-coil motif.";
RL Nucleic Acids Res. 38:4040-4051(2010).
CC -!- FUNCTION: Stimulates transcription elongation. {ECO:0000255|HAMAP-
CC Rule:MF_00950, ECO:0000269|PubMed:20197319}.
CC -!- SUBUNIT: Heterodimer composed of Spt4 and Spt5. Interacts with RNA
CC polymerase (RNAP). Forms a homodimer in solution. {ECO:0000255|HAMAP-
CC Rule:MF_00950, ECO:0000269|PubMed:19475703,
CC ECO:0000269|PubMed:20197319}.
CC -!- INTERACTION:
CC Q57818; Q57839: spt4; NbExp=3; IntAct=EBI-15739382, EBI-15739363;
CC -!- DOMAIN: Composed of only a NusG N-terminal (NGN) domain and a KOW
CC domain, similar to bacterial NusG. The NGN domain is the effector
CC domain of the complex that mediates the interaction with RNAP and is
CC essential for elongation activity. {ECO:0000269|PubMed:19475703,
CC ECO:0000269|PubMed:20197319}.
CC -!- SIMILARITY: Belongs to the archaeal Spt5 family. {ECO:0000255|HAMAP-
CC Rule:MF_00950}.
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DR EMBL; L77117; AAB98361.1; -; Genomic_DNA.
DR PIR; D64346; D64346.
DR RefSeq; WP_010869871.1; NC_000909.1.
DR PDB; 3EWG; X-ray; 2.04 A; A=1-83.
DR PDB; 3LPE; X-ray; 1.90 A; A/C/E/G=1-82.
DR PDB; 4ZN1; X-ray; 2.80 A; A=1-147.
DR PDB; 4ZN3; X-ray; 2.30 A; A=1-147.
DR PDBsum; 3EWG; -.
DR PDBsum; 3LPE; -.
DR PDBsum; 4ZN1; -.
DR PDBsum; 4ZN3; -.
DR AlphaFoldDB; Q57818; -.
DR SMR; Q57818; -.
DR DIP; DIP-46333N; -.
DR IntAct; Q57818; 1.
DR STRING; 243232.MJ_0372; -.
DR EnsemblBacteria; AAB98361; AAB98361; MJ_0372.
DR GeneID; 1451229; -.
DR KEGG; mja:MJ_0372; -.
DR eggNOG; arCOG01920; Archaea.
DR HOGENOM; CLU_113589_0_0_2; -.
DR InParanoid; Q57818; -.
DR OMA; FSEIEHF; -.
DR OrthoDB; 91936at2157; -.
DR PhylomeDB; Q57818; -.
DR EvolutionaryTrace; Q57818; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.70.940; -; 1.
DR HAMAP; MF_00950; Spt5_arch; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR011590; Spt5_arc.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR SMART; SM00739; KOW; 1.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR00405; KOW_elon_Spt5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..147
FT /note="Transcription elongation factor Spt5"
FT /id="PRO_0000113978"
FT DOMAIN 91..122
FT /note="KOW"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00950"
FT MUTAGEN 4
FT /note="A->R: Abrogates binding to RNAP. Decreases
FT elongation activity."
FT /evidence="ECO:0000269|PubMed:20197319"
FT MUTAGEN 42
FT /note="Y->A: Abrogates binding to RNAP. Decreases
FT elongation activity."
FT /evidence="ECO:0000269|PubMed:20197319"
FT MUTAGEN 44
FT /note="L->A: Can still bind RNAP, but with a decreased
FT affinity. Does not affect elongation activity."
FT /evidence="ECO:0000269|PubMed:20197319"
FT MUTAGEN 44
FT /note="L->R: Abrogates binding to RNAP. Decreases
FT elongation activity."
FT /evidence="ECO:0000269|PubMed:20197319"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3LPE"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3LPE"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3LPE"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:3LPE"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:3LPE"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3LPE"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:3LPE"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:4ZN3"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:4ZN3"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:4ZN3"
FT TURN 114..117
FT /evidence="ECO:0007829|PDB:4ZN3"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:4ZN3"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:4ZN3"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4ZN3"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4ZN3"
SQ SEQUENCE 147 AA; 16136 MW; A8D917571BF5F215 CRC64;
MIFAVRTMVG QEKNIAGLMA SRAEKEQLDV YSILASESLK GYVLVEAETK GDVEELIKGM
PRVRGIVPGT IAIEEIEPLL TPKKIIENIE KGDVVEIIAG PFKGERAKVI RVDKHKEEVT
LELENAAVPI PITLPVEGVK IVSKHKD
