TSAB_SALTY
ID TSAB_SALTY Reviewed; 231 AA.
AC Q7CQE0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB;
DE AltName: Full=Resuscitation-promoting factor;
DE Short=RPF;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB;
GN Name=tsaB; Synonyms=rpf, yeaZ; OrderedLocusNames=STM1820;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP IDENTIFICATION AS A RESUSCITATION-PROMOTING FACTOR.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=16213054; DOI=10.1016/j.ijfoodmicro.2005.06.022;
RA Panutdaporn N., Kawamoto K., Asakura H., Makino S.I.;
RT "Resuscitation of the viable but non-culturable state of Salmonella
RT enterica serovar Oranienburg by recombinant resuscitation-promoting factor
RT derived from Salmonella Typhimurium strain LT2.";
RL Int. J. Food Microbiol. 106:241-247(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), LACK OF NUCLEOTIDE-BINDING, AND
RP LACK OF GLYCOPROTEASE ACTIVITY.
RC STRAIN=SL3261;
RX PubMed=16617437; DOI=10.1002/prot.20982;
RA Nichols C.E., Johnson C., Lockyer M., Charles I.G., Lamb H.K.,
RA Hawkins A.R., Stammers D.K.;
RT "Structural characterization of Salmonella typhimurium YeaZ, an M22 O-
RT sialoglycoprotein endopeptidase homolog.";
RL Proteins 64:111-123(2006).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is involved in the transfer of the threonylcarbamoyl
CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC together with TsaD and TsaE; this reaction does not require ATP in
CC vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis
CC pathway, possibly in regulating the core enzymatic function of TsaD (By
CC similarity). Neither binds polyphosphates nor a wide range of
CC nucleotides on its own. Does not show O-sialoglycoprotein endopeptidase
CC activity. {ECO:0000250}.
CC -!- FUNCTION: Has been identified as the first Gram-negative bacterial RPF
CC (Resuscitation-Promoting Factor) capable of reviving VNC (viable but
CC non-culturable) cells when added externally, but the million-fold lower
CC activity as compared to Gram-positive bacterial RPFs may indicate a
CC lack of physiological relevance. {ECO:0000269|PubMed:16213054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL20735.1; -; Genomic_DNA.
DR RefSeq; NP_460776.1; NC_003197.2.
DR RefSeq; WP_001221014.1; NC_003197.2.
DR PDB; 2GEL; X-ray; 2.05 A; A/G=1-231.
DR PDB; 2GEM; X-ray; 2.10 A; A/B=1-231.
DR PDBsum; 2GEL; -.
DR PDBsum; 2GEM; -.
DR AlphaFoldDB; Q7CQE0; -.
DR PCDDB; Q7CQE0; -.
DR SMR; Q7CQE0; -.
DR STRING; 99287.STM1820; -.
DR PaxDb; Q7CQE0; -.
DR EnsemblBacteria; AAL20735; AAL20735; STM1820.
DR GeneID; 1253339; -.
DR KEGG; stm:STM1820; -.
DR PATRIC; fig|99287.12.peg.1920; -.
DR HOGENOM; CLU_064886_2_0_6; -.
DR OMA; DEVYWGC; -.
DR PhylomeDB; Q7CQE0; -.
DR BioCyc; SENT99287:STM1820-MON; -.
DR EvolutionaryTrace; Q7CQE0; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR022496; T6A_TsaB.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF11; PTHR11735:SF11; 1.
DR Pfam; PF00814; TsaD; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR03725; T6A_YeaZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; tRNA processing.
FT CHAIN 1..231
FT /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT TsaB"
FT /id="PRO_0000423847"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 9..19
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:2GEL"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:2GEL"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:2GEL"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:2GEL"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2GEL"
SQ SEQUENCE 231 AA; 24742 MW; A5AF585D5B6DA15D CRC64;
MRILAIDTAT EACSVALWNN GTINAHFELC PREHTQRILP MVQEILAASG ASLNEIDALA
FGRGPGSFTG VRIGIGIAQG LALGANLPMI GVSTLATMAQ GAWRKTGATR VLAAIDARMG
EVYWAEYQRD AQGVWQGEET EAVLKPERVG ERLKQLSGEW ATVGTGWSAW PDLAKECGLT
LHDGEVSLPA AEDMLPIASQ KLAAGETVAV EHAEPVYLRN EVAWKKLPGK E
