TSAB_VIBPA
ID TSAB_VIBPA Reviewed; 233 AA.
AC Q87RD1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaB;
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB;
GN Name=tsaB; Synonyms=yeaZ; OrderedLocusNames=VP0866;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=ATCC 43996 / DSM 11058 / NCTC 10884;
RX PubMed=21543872; DOI=10.1107/s1744309111010219;
RA Aydin I., Dimitropoulos A., Chen S.H., Thomas C., Roujeinikova A.;
RT "Purification, crystallization and preliminary X-ray crystallographic
RT analysis of the putative Vibrio parahaemolyticus resuscitation-promoting
RT factor YeaZ.";
RL Acta Crystallogr. F 67:604-607(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 2-214, SUBUNIT, AND DIMERIZATION
RP MODE.
RC STRAIN=ATCC 43996 / DSM 11058 / NCTC 10884;
RX PubMed=21858042; DOI=10.1371/journal.pone.0023245;
RA Aydin I., Saijo-Hamano Y., Namba K., Thomas C., Roujeinikova A.;
RT "Structural analysis of the essential resuscitation promoting factor YeaZ
RT suggests a mechanism of nucleotide regulation through dimer
RT reorganization.";
RL PLoS ONE 6:E23245-E23245(2011).
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). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21543872,
CC ECO:0000269|PubMed:21858042}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Structural analysis identified two distinctly different
CC modes of TsaB dimer formation. In one form, prevalent in the absence of
CC nucleotide, the putative nucleotide-binding site is incomplete and
CC lacks a binding pocket for a nucleotide base. In the second form, an
CC interface between the two subunits apparently completes a nucleotide-
CC binding site. This analysis suggests that the two dimer architectures
CC observed in the crystal structures correspond to a free and a
CC nucleotide-bound form of TsaB. This suggests that nucleotide binding to
CC TsaB acts as a regulator or a switch that changes the shape of TsaB and
CC allows it to interact with different partner proteins
CC (PubMed:21858042). {ECO:0000305|PubMed:21858042}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. TsaB subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000031; BAC59129.1; -; Genomic_DNA.
DR RefSeq; NP_797245.1; NC_004603.1.
DR RefSeq; WP_005478795.1; NC_004603.1.
DR PDB; 3R6M; X-ray; 3.10 A; A/B/C/D=2-214.
DR PDBsum; 3R6M; -.
DR AlphaFoldDB; Q87RD1; -.
DR SMR; Q87RD1; -.
DR STRING; 223926.28805853; -.
DR EnsemblBacteria; BAC59129; BAC59129; BAC59129.
DR GeneID; 1188363; -.
DR KEGG; vpa:VP0866; -.
DR PATRIC; fig|223926.6.peg.819; -.
DR eggNOG; COG1214; Bacteria.
DR HOGENOM; CLU_064886_2_0_6; -.
DR OMA; DEVYWGC; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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..233
FT /note="tRNA threonylcarbamoyladenosine biosynthesis protein
FT TsaB"
FT /id="PRO_0000423849"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 11..23
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3R6M"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:3R6M"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:3R6M"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:3R6M"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3R6M"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:3R6M"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3R6M"
FT TURN 167..171
FT /evidence="ECO:0007829|PDB:3R6M"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3R6M"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3R6M"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:3R6M"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3R6M"
SQ SEQUENCE 233 AA; 25151 MW; 8827932C4CAC5DD9 CRC64;
MSAKILAIDT ATENCSVALL VNDQVISRSE VAPRDHTKKV LPMVDEVLKE AGLTLQDLDA
LAFGRGPGSF TGVRIGIGIA QGLAFGAELP MIGVSTLAAM AQASYRLHGA TDVAVAIDAR
MSEVYWARYS RQENGEWIGV DEECVIPPAR LAEEAQADSK TWTTAGTGWS AYQEELAGLP
FNTADSEVLY PDSQDIVILA KQELEKGNTV PVEESSPVYL RDNVTWKKLP GRE
