TATAO_HALVD
ID TATAO_HALVD Reviewed; 90 AA.
AC D4GVK4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Sec-independent protein translocase protein TatAo {ECO:0000255|HAMAP-Rule:MF_00236};
GN Name=tatAo {ECO:0000255|HAMAP-Rule:MF_00236}; OrderedLocusNames=HVO_1027;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=DS2 / DS70 / H99;
RX PubMed=16291683; DOI=10.1128/jb.187.23.8104-8113.2005;
RA Dilks K., Gimenez M.I., Pohlschroder M.;
RT "Genetic and biochemical analysis of the twin-arginine translocation
RT pathway in halophilic archaea.";
RL J. Bacteriol. 187:8104-8113(2005).
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. TatA could
CC form the protein-conducting channel of the Tat system (Probable).
CC {ECO:0000305|PubMed:16291683}.
CC -!- SUBUNIT: Forms a complex with TatC (By similarity). Cytoplasmic and
CC membrane-bound TatA form high-molecular-weight complexes.
CC {ECO:0000255|HAMAP-Rule:MF_00236, ECO:0000269|PubMed:16291683}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00236,
CC ECO:0000269|PubMed:16291683}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00236, ECO:0000269|PubMed:16291683}.
CC Cytoplasm {ECO:0000269|PubMed:16291683}.
CC -!- MISCELLANEOUS: H.volcanii possesses two TatA translocases: TatAo and
CC TatAt. Each may interact with specific Tat substrates
CC (PubMed:16291683). {ECO:0000305|PubMed:16291683}.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC Rule:MF_00236}.
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DR EMBL; CP001956; ADE04997.1; -; Genomic_DNA.
DR RefSeq; WP_004043915.1; NZ_AOHU01000092.1.
DR AlphaFoldDB; D4GVK4; -.
DR SMR; D4GVK4; -.
DR STRING; 309800.C498_13624; -.
DR TCDB; 2.A.64.4.1; the twin arginine targeting (tat) family.
DR EnsemblBacteria; ADE04997; ADE04997; HVO_1027.
DR GeneID; 8924188; -.
DR KEGG; hvo:HVO_1027; -.
DR eggNOG; arCOG02694; Archaea.
DR HOGENOM; CLU_086034_3_3_2; -.
DR OMA; IMGDIPG; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR Pfam; PF02416; TatA_B_E; 1.
DR TIGRFAMs; TIGR01411; tatAE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..90
FT /note="Sec-independent protein translocase protein TatAo"
FT /id="PRO_0000417358"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT REGION 39..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 90 AA; 9583 MW; 6A2B39BAC0E8F6ED CRC64;
MLDSIPLFPG LPGGPELLIV LLIVVLLFGA NKLPQLARSS GQAMGEFRRG REEIEEELKK
GAEGGDDEGE NGDEAEADDA DATETEAESR