(data stored in SCRATCH zone)

SWISSPROT: C8W4U8_DESAS

ID   C8W4U8_DESAS            Unreviewed;       320 AA.
AC   C8W4U8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 58.
DE   SubName: Full=ABC transporter related {ECO:0000313|EMBL:ACV61300.1};
GN   OrderedLocusNames=Dtox_0347 {ECO:0000313|EMBL:ACV61300.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61300.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61300.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000256|SAAS:SAAS00555009}.
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DR   EMBL; CP001720; ACV61300.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0347; -.
DR   EnsemblBacteria; ACV61300; ACV61300; Dtox_0347.
DR   KEGG; dae:Dtox_0347; -.
DR   eggNOG; ENOG4108JQ7; Bacteria.
DR   eggNOG; COG4608; LUCA.
DR   KO; K10824; -.
DR   OMA; VNPRMTA; -.
DR   BioCyc; DACE485916:G1GFV-363-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0015833; P:peptide transport; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W4U8.
DR   SWISS-2DPAGE; C8W4U8.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00554975};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434,
KW   ECO:0000256|SAAS:SAAS00554985};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transport {ECO:0000256|SAAS:SAAS00554993}.
FT   DOMAIN        4    253       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND      46     53       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   320 AA;  35884 MW;  33F6158B2D91DBC6 CRC64;
     MSLLEINNIT KTFSLGNKFL KTNQSIAAVK DISLSLEEGC CLGIVGESGC GKTTLGKIIL
     GLEKPERGEV FFLGKDIYQT TGRELKELRR NLQVVFQDSL SAVNPRLPIG KIISEPIRNY
     RKLTPSEEKK QVLELLEIVG LSPADIDKYP HQFSGGQIQR VTIARAIALK PKLIVLDEAV
     ASLDMSVQAQ ILNLLLDLKE EFKLSYIFIS HDILAVNYIS DRLAVMYMGK VVELIEDIRL
     IDELRHPYSI KLLSSVLSDH PRHRKKLSSS FDEPAISENG SYGCSYFTRC EKASVLCREQ
     TPLLSSLKEK HKVACPYCTR
//

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