TATA_SACEN
ID TATA_SACEN Reviewed; 90 AA.
AC A4FBZ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000255|HAMAP-Rule:MF_00236};
GN Name=tatA {ECO:0000255|HAMAP-Rule:MF_00236}; OrderedLocusNames=SACE_2262;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00236}.
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_00236}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00236};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00236}.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000255|HAMAP-
CC Rule:MF_00236}.
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DR EMBL; AM420293; CAM01567.1; -; Genomic_DNA.
DR RefSeq; WP_009945846.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FBZ2; -.
DR SMR; A4FBZ2; -.
DR STRING; 405948.SACE_2262; -.
DR EnsemblBacteria; CAM01567; CAM01567; SACE_2262.
DR KEGG; sen:SACE_2262; -.
DR eggNOG; COG1826; Bacteria.
DR HOGENOM; CLU_086034_4_0_11; -.
DR OMA; WHWLILA; -.
DR OrthoDB; 1907955at2; -.
DR Proteomes; UP000006728; 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_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR Pfam; PF02416; TatA_B_E; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..90
FT /note="Sec-independent protein translocase protein TatA"
FT /id="PRO_0000336643"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00236"
FT REGION 42..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 90 AA; 9666 MW; 6E80E8B5E29BE42E CRC64;
MGLPGGWELV LIVGVLVLLF GATKLPQMAR SLGQSARVFK AEARGMKEDE EAAKREKQAK
SEPQQLTAGE SSAPTVASPV EETQRNDSKK
