ID L0K3K9_9EURY Unreviewed; 326 AA.
AC L0K3K9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Sec-independent protein translocase protein TatC {ECO:0000256|HAMAP-Rule:MF_00902};
GN Name=tatC {ECO:0000256|HAMAP-Rule:MF_00902};
GN ORFNames=Natoc_3906 {ECO:0000313|EMBL:AGB39606.1};
OS Natronococcus occultus SP4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronococcus.
OX NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB39606.1, ECO:0000313|Proteomes:UP000010878};
RN [1] {ECO:0000313|EMBL:AGB39606.1, ECO:0000313|Proteomes:UP000010878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP4 {ECO:0000313|EMBL:AGB39606.1,
RC ECO:0000313|Proteomes:UP000010878};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA Klenk H.-P.;
RT "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|HAMAP-Rule:MF_00902}.
CC -!- SUBUNIT: Forms a complex with TatA. {ECO:0000256|HAMAP-Rule:MF_00902}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00902}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000256|HAMAP-
CC Rule:MF_00902}.
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DR EMBL; CP003929; AGB39606.1; -; Genomic_DNA.
DR RefSeq; WP_015323040.1; NC_019974.1.
DR AlphaFoldDB; L0K3K9; -.
DR STRING; 694430.Natoc_3906; -.
DR GeneID; 14402917; -.
DR KEGG; nou:Natoc_3906; -.
DR eggNOG; arCOG01919; Archaea.
DR eggNOG; arCOG06180; Archaea.
DR HOGENOM; CLU_031942_8_1_2; -.
DR OrthoDB; 198870at2157; -.
DR Proteomes; UP000010878; Chromosome.
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_00902; TatC; 1.
DR InterPro; IPR002033; TatC.
DR PANTHER; PTHR30371; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC; 1.
DR PANTHER; PTHR30371:SF0; SEC-INDEPENDENT PROTEIN TRANSLOCASE PROTEIN TATC, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00902; TatC; 1.
DR PRINTS; PR01840; TATCFAMILY.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00902};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00902};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_00902};
KW Reference proteome {ECO:0000313|Proteomes:UP000010878};
KW Translocation {ECO:0000256|HAMAP-Rule:MF_00902};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00902};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00902}; Transport {ECO:0000256|HAMAP-Rule:MF_00902}.
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 193..224
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 244..269
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 281..296
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00902"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..58
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 35878 MW; D8B2789EF148AD68 CRC64;
MSDESATDGD VEPPEEPRDE PAAEGSSDAD SEPADDGTAG DDGALESADD EEPELETDGE
GIVGDRQEES EPAYPDPDDD VGGISTPPDD EEMPLADHIE EMVLRLAVVF LVGAAGTAIG
LLWASQAIDH VWHNVFPSQF EQVPPPHIYH PLELWLTRIK LSALLGIMVA LPMFVYQCYL
FMKPGLYPNE RKYYLAAVPT SVVLGALGMI FSYLLVLPIL FQYFTFYAEG SAGIAYALGD
TFDLIITLTG FLAIVFQIPL FMMLAIMMGV TTRKWLESKR LYFWAGFAGL SFMFTVDPTM
MAPILVAVTM ILLFEGTLLL LRWTGR
//
