ID L9XIH0_9EURY Unreviewed; 84 AA.
AC L9XIH0;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Sec-independent protein translocase protein TatA {ECO:0000256|HAMAP-Rule:MF_00236};
GN Name=tatA {ECO:0000256|HAMAP-Rule:MF_00236};
GN ORFNames=C493_02843 {ECO:0000313|EMBL:ELY61216.1};
OS Natronolimnohabitans innermongolicus JCM 12255.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnohabitans.
OX NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY61216.1, ECO:0000313|Proteomes:UP000011602};
RN [1] {ECO:0000313|EMBL:ELY61216.1, ECO:0000313|Proteomes:UP000011602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY61216.1,
RC ECO:0000313|Proteomes:UP000011602};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:0000256|HAMAP-Rule:MF_00236}.
CC -!- SUBUNIT: Forms a complex with TatC. {ECO:0000256|HAMAP-Rule:MF_00236}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00236};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00236}.
CC -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000256|HAMAP-
CC Rule:MF_00236}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY61216.1}.
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DR EMBL; AOHZ01000014; ELY61216.1; -; Genomic_DNA.
DR RefSeq; WP_007257879.1; NZ_AOHZ01000014.1.
DR AlphaFoldDB; L9XIH0; -.
DR STRING; 1227499.C493_02843; -.
DR PATRIC; fig|1227499.3.peg.583; -.
DR eggNOG; arCOG02694; Archaea.
DR Proteomes; UP000011602; Unassembled WGS sequence.
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 Gene3D; 1.20.5.3310; -; 1.
DR HAMAP; MF_00236; TatA_E; 1.
DR InterPro; IPR003369; TatA/B/E.
DR InterPro; IPR006312; TatA/E.
DR NCBIfam; TIGR01411; tatAE; 1.
DR PANTHER; PTHR42982; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA; 1.
DR PANTHER; PTHR42982:SF7; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATA; 1.
DR Pfam; PF02416; TatA_B_E; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00236};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_00236}; Reference proteome {ECO:0000313|Proteomes:UP000011602};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00236};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00236}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00236"
FT REGION 44..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 84 AA; 8874 MW; 760E49C629922D9C CRC64;
MTSLAPLFAP IPGGPELLII VGIAILLFGA QKIPKLARSI GESTGEFKKG QAKVENELEE
LRDPTTEVDS SAETQPATEA QPES
//
