TATCT_HALVD
ID TATCT_HALVD Reviewed; 718 AA.
AC D4GZC9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Sec-independent protein translocase protein TatCt {ECO:0000255|HAMAP-Rule:MF_00902};
GN Name=tatCt {ECO:0000255|HAMAP-Rule:MF_00902}; OrderedLocusNames=HVO_0185;
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, 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.
CC {ECO:0000305|PubMed:16291683}.
CC -!- SUBUNIT: Forms a complex with TatA. {ECO:0000255|HAMAP-Rule:MF_00902}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00902,
CC ECO:0000269|PubMed:16291683}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00902, ECO:0000269|PubMed:16291683}.
CC -!- MISCELLANEOUS: H.volcanii possesses two TatC translocases: TatCo and
CC TatCt. Both paralogs are structurally atypical and may represent
CC adaptation to the extensive utilization of the Tat pathway in
CC haloarchaea (PubMed:16291683). {ECO:0000305|PubMed:16291683}.
CC -!- SIMILARITY: Belongs to the TatC family. {ECO:0000255|HAMAP-
CC Rule:MF_00902}.
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DR EMBL; CP001956; ADE02320.1; -; Genomic_DNA.
DR RefSeq; WP_004045299.1; NZ_AOHU01000106.1.
DR AlphaFoldDB; D4GZC9; -.
DR SMR; D4GZC9; -.
DR STRING; 309800.C498_19179; -.
DR TCDB; 2.A.64.5.1; the twin arginine targeting (tat) family.
DR EnsemblBacteria; ADE02320; ADE02320; HVO_0185.
DR GeneID; 8926452; -.
DR KEGG; hvo:HVO_0185; -.
DR eggNOG; arCOG04736; Archaea.
DR HOGENOM; CLU_359694_0_0_2; -.
DR OMA; RDKWRHA; -.
DR OrthoDB; 13074at2157; -.
DR Proteomes; UP000008243; 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_00902; TatC; 1.
DR InterPro; IPR002033; TatC.
DR PANTHER; PTHR30371; PTHR30371; 2.
DR Pfam; PF00902; TatC; 2.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..718
FT /note="Sec-independent protein translocase protein TatCt"
FT /id="PRO_0000417361"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 214..231
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 661..681
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT REGION 421..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 77986 MW; 6883944B098C7DA7 CRC64;
MSSALDEDTQ QTIAAGRETA GAMLRAAQKD LQKVFIVFLV GFLGTFYALR LYVWEFFRGV
TKAQMDASVS GNVSIIAQTP FDVILLQAKI GLVVGVLFAL PPFIYVSRGA LKARDAWPKS
PVAPWKLALI GLTMVALFAA GVAYGYFVFF PFTFAFLAQN AISAGFTPSY SIVKWAQFIF
LLTLSFGLAS QLPLAMTGLS YAEVVPYELF RDKWRHAIVG IFAFGALFTP PDPFTQIMWA
VPVILLYAFS LYLARVVVTA KRGSEKIDVK STATTHWNLL AGVGVVVGLL VYAFYEYGGV
ELANDGLAAI GSDYVFLAPG SGVALGAFVV AGGFVGLAFG LAYLVYRDIE RLERTEIGVG
DPTKLDLSAL DVAGVRAAPP EAFADLEEDE VMALASAAID DGDKAKAQAL IDRFDEAEAD
REAEAADAED EPGELEDRTT RAGGAFVSEL TEGETDEDDI GGYYTDIAFI VDSLTSRAFW
VVGWFMLVLA TTFGWLYTGG IRDVYDDFLG RLPAAVRPEE VLNVVALHPM EALIFEVKFS
TILAVLATLP LVAYFVWPAL RERNIIRKRR RTVFVWTGAL AGGLLGGFAL GYTYVAPTVI
TFLVEDALAA NMIITYRITN FFWLIFFTTA GIGLLADVPI LMVLLNTAGI SYRMMRNRWR
EVTVFILAIS AVFTPASITT MFMVTLPLMA AYGVGLGVLF VLTVGGRRDL SPARGAAE
