TATB_ZYMMO
ID TATB_ZYMMO Reviewed; 152 AA.
AC Q5NN67;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Sec-independent protein translocase protein TatB {ECO:0000255|HAMAP-Rule:MF_00237};
GN Name=tatB {ECO:0000255|HAMAP-Rule:MF_00237}; OrderedLocusNames=ZMO1219;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [2]
RP SEQUENCE REVISION TO 8.
RX PubMed=19816441; DOI=10.1038/nbt1009-893;
RA Yang S., Pappas K.M., Hauser L.J., Land M.L., Chen G.L., Hurst G.B.,
RA Pan C., Kouvelis V.N., Typas M.A., Pelletier D.A., Klingeman D.M.,
RA Chang Y.J., Samatova N.F., Brown S.D.;
RT "Improved genome annotation for Zymomonas mobilis.";
RL Nat. Biotechnol. 27:893-894(2009).
CC -!- FUNCTION: Part of the twin-arginine translocation (Tat) system that
CC transports large folded proteins containing a characteristic twin-
CC arginine motif in their signal peptide across membranes. Together with
CC TatC, TatB is part of a receptor directly interacting with Tat signal
CC peptides. TatB may form an oligomeric binding site that transiently
CC accommodates folded Tat precursor proteins before their translocation.
CC {ECO:0000255|HAMAP-Rule:MF_00237}.
CC -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC
CC complex, containing multiple copies of TatA, TatB and TatC subunits,
CC and a separate TatA complex, containing only TatA subunits. Substrates
CC initially bind to the TatABC complex, which probably triggers
CC association of the separate TatA complex to form the active translocon.
CC {ECO:0000255|HAMAP-Rule:MF_00237}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00237}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00237}.
CC -!- SIMILARITY: Belongs to the TatB family. {ECO:0000255|HAMAP-
CC Rule:MF_00237}.
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DR EMBL; AE008692; AAV89843.2; -; Genomic_DNA.
DR RefSeq; WP_011241037.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NN67; -.
DR SMR; Q5NN67; -.
DR STRING; 264203.ZMO1219; -.
DR EnsemblBacteria; AAV89843; AAV89843; ZMO1219.
DR GeneID; 58026989; -.
DR KEGG; zmo:ZMO1219; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_1_3_5; -.
DR OMA; FDIAWTE; -.
DR OrthoDB; 2073616at2; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0033281; C:TAT protein transport complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043953; P:protein transport by the Tat complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00237; TatB; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR018448; TatB.
DR Pfam; PF02416; TatA_B_E; 1.
DR TIGRFAMs; TIGR01410; tatB; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..152
FT /note="Sec-independent protein translocase protein TatB"
FT /id="PRO_0000301256"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00237"
FT REGION 60..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 152 AA; 16466 MW; 334C49991AA53CF6 CRC64;
MFDVAPSELL LVAVVALVVI GPKDLPRAMR VVGRWLGKAR KLSRHFRSGI DEMIRQSEME
DMEKRWAEEN AKLLAENQGQ GNQTASTSSP ATPSPVSDDP AEQNIVFTSP ADLEVNTADT
SHLAANHTET TATTAASTPA KPKEADQQEK QS