(data stored in SCRATCH zone)

SWISSPROT: Q2IM07_ANADE

ID   Q2IM07_ANADE            Unreviewed;       146 AA.
AC   Q2IM07;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   07-NOV-2018, entry version 88.
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   OrderedLocusNames=Adeh_0060 {ECO:0000313|EMBL:ABC79838.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79838.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|EMBL:ABC79838.1, ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|EMBL:ABC79838.1,
RC   ECO:0000313|Proteomes:UP000001935};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the twin-arginine translocation (Tat) system
CC       that transports large folded proteins containing a characteristic
CC       twin-arginine motif in their signal peptide across membranes. TatA
CC       could form the protein-conducting channel of the Tat system.
CC       {ECO:0000256|HAMAP-Rule:MF_00236, ECO:0000256|SAAS:SAAS01089842}.
CC   -!- SUBUNIT: The Tat system comprises two distinct complexes: a TatABC
CC       complex, containing multiple copies of TatA, TatB and TatC
CC       subunits, and a separate TatA complex, containing only TatA
CC       subunits. Substrates initially bind to the TatABC complex, which
CC       probably triggers association of the separate TatA complex to form
CC       the active translocon. {ECO:0000256|HAMAP-Rule:MF_00236}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00236}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00236}.
CC   -!- SIMILARITY: Belongs to the TatA/E family. {ECO:0000256|HAMAP-
CC       Rule:MF_00236, ECO:0000256|SAAS:SAAS01089839}.
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DR   EMBL; CP000251; ABC79838.1; -; Genomic_DNA.
DR   RefSeq; WP_011419121.1; NC_007760.1.
DR   STRING; 290397.Adeh_0060; -.
DR   EnsemblBacteria; ABC79838; ABC79838; Adeh_0060.
DR   KEGG; ade:Adeh_0060; -.
DR   eggNOG; ENOG41067S4; Bacteria.
DR   eggNOG; ENOG410XUF0; LUCA.
DR   HOGENOM; HOG000002567; -.
DR   KO; K03117; -.
DR   OMA; NEAQHEG; -.
DR   BioCyc; ADEH290397:G1G5W-62-MONOMER; -.
DR   Proteomes; UP000001935; 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:0009306; P:protein secretion; IEA:InterPro.
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; MttA_Hcf106; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IM07.
DR   SWISS-2DPAGE; Q2IM07.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00236};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01089845};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01091839};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01091841};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01091833};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01091830};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01091829};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00236,
KW   ECO:0000256|SAAS:SAAS01091840}.
SQ   SEQUENCE   146 AA;  14534 MW;  D14BF0752D5E36FA CRC64;
     MFGLSFGEIV IIAVLALILL GPDRLPEAAK TIGKGLRQFK QATDDLKDQI ETEIYKDDRK
     VARPSLVPPV PNRPVPGPAG PPPAATAENV PGLEAALVDA EPAASAVEPA AAAAQPAAVA
     TAPAPSPSPE PSGEGAPPPG TGGTAA
//

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