ID   TUSB_PECPM              Reviewed;          95 AA.
AC   Q5XWD9; K4FN52;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Protein TusB {ECO:0000255|HAMAP-Rule:MF_01564};
DE   AltName: Full=tRNA 2-thiouridine synthesizing protein B {ECO:0000255|HAMAP-Rule:MF_01564};
GN   Name=tusB {ECO:0000255|HAMAP-Rule:MF_01564}; OrderedLocusNames=W5S_4168;
OS   Pectobacterium parmentieri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=1905730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCC3193;
RX   PubMed=15668006; DOI=10.1016/j.femsle.2004.11.045;
RA   Laasik E., Ojarand M., Pajunen M., Savilahti H., Maee A.;
RT   "Novel mutants of Erwinia carotovora subsp. carotovora defective in the
RT   production of plant cell wall degrading enzymes generated by Mu
RT   transpososome-mediated insertion mutagenesis.";
RL   FEMS Microbiol. Lett. 243:93-99(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCC3193;
RX   PubMed=23045508; DOI=10.1128/jb.00681-12;
RA   Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P.,
RA   Paulin L., Pirhonen M., Palva T., Holm L.;
RT   "Genome sequence of Pectobacterium sp. strain SCC3193.";
RL   J. Bacteriol. 194:6004-6004(2012).
CC   -!- FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5-
CC       methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions.
CC       {ECO:0000255|HAMAP-Rule:MF_01564}.
CC   -!- SUBUNIT: Heterohexamer, formed by a dimer of trimers. The hexameric
CC       TusBCD complex contains 2 copies each of TusB, TusC and TusD. The
CC       TusBCD complex interacts with TusE. {ECO:0000255|HAMAP-Rule:MF_01564}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01564}.
CC   -!- SIMILARITY: Belongs to the DsrH/TusB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01564}.
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DR   EMBL; AY730616; AAU44790.1; -; Genomic_DNA.
DR   EMBL; CP003415; AFI92224.1; -; Genomic_DNA.
DR   RefSeq; WP_014701623.1; NZ_QESW01000010.1.
DR   AlphaFoldDB; Q5XWD9; -.
DR   SMR; Q5XWD9; -.
DR   STRING; 1905730.W5S_4168; -.
DR   EnsemblBacteria; AFI92224; AFI92224; W5S_4168.
DR   KEGG; pec:W5S_4168; -.
DR   eggNOG; COG2168; Bacteria.
DR   HOGENOM; CLU_166087_2_1_6; -.
DR   OMA; MLHTINK; -.
DR   OrthoDB; 1995110at2; -.
DR   Proteomes; UP000008044; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:InterPro.
DR   Gene3D; 3.40.1260.10; -; 1.
DR   HAMAP; MF_01564; Thiourid_synth_B; 1.
DR   InterPro; IPR027396; DsrEFH-like.
DR   InterPro; IPR023526; Sulphur_relay_TusB.
DR   InterPro; IPR007215; Sulphur_relay_TusB/DsrH.
DR   PANTHER; PTHR37526; PTHR37526; 1.
DR   Pfam; PF04077; DsrH; 1.
DR   SUPFAM; SSF75169; SSF75169; 1.
DR   TIGRFAMs; TIGR03011; sulf_tusB_dsrH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; tRNA processing.
FT   CHAIN           1..95
FT                   /note="Protein TusB"
FT                   /id="PRO_0000234514"
SQ   SEQUENCE   95 AA;  10458 MW;  4BA9E25627633E18 CRC64;
     MLHTLSSSPY HADLDTLLRS VDEGDALVLL QDGVIAALAG GDIIHRLLAS AVFLYVLRPD
     TEARGMTEQI SNNVALIDYN EFVQLTVEHP QQLAW