TATCO_HALVD
ID TATCO_HALVD Reviewed; 441 AA.
AC D4GZD0;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Sec-independent protein translocase protein TatCo {ECO:0000255|HAMAP-Rule:MF_00902};
GN Name=tatCo {ECO:0000255|HAMAP-Rule:MF_00902}; OrderedLocusNames=HVO_0186;
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; ADE04167.1; -; Genomic_DNA.
DR RefSeq; WP_004045300.1; NZ_AOHU01000106.1.
DR AlphaFoldDB; D4GZD0; -.
DR STRING; 309800.C498_19184; -.
DR TCDB; 2.A.64.4.1; the twin arginine targeting (tat) family.
DR EnsemblBacteria; ADE04167; ADE04167; HVO_0186.
DR GeneID; 8923939; -.
DR KEGG; hvo:HVO_0186; -.
DR eggNOG; arCOG01919; Archaea.
DR HOGENOM; CLU_031942_8_0_2; -.
DR OrthoDB; 42213at2157; -.
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; 1.
DR Pfam; PF00902; TatC; 1.
DR PRINTS; PR01840; TATCFAMILY.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..441
FT /note="Sec-independent protein translocase protein TatCo"
FT /id="PRO_0000417360"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00902"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..100
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 46844 MW; 0091F26D3326349F CRC64;
MADEERDAGL SAADDETDAS DDTDQRSSDG DADDADDASS SSDGPVYGRV TPRDETVTHG
SDDDASADVA AETGDNGDDS DSDTDAAPDD ADDSATDSDA DSDDEPRLLA DDEHTSHVPE
GTYDDSSDES ADDVDPDAAA DGASPALTGE DEMGGVAPSS VSAEDADFDD EDVGGLVGEA
PESDQEMPLT AHIEEMIRRL AVVLGVAGAI TLVLFPGADI LNALVDTQAA FGVHIPSATD
VINFLWNSHI PGAETIVDRR PRLYGPLELI LTKLKVAGLA GTVIGLPVFV YETYLFMRPG
LYPKERKYYL AAVPTSLVLA LVGVLFAHFV VLPAIFAYFT SYTEGTAVVA FGLKETFNLI
LILMGYMAVV FQIPLFVELA IMMNLVTRRW LEDRRLLFWG AFLGLAFLVS PDPTGMAPII
IGATMITLFE GTLAALRWTG N