Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]

MULTISPECIES: ABC transporter permease [Salmonella].


LOCUS       WP_000998823             256 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_000998823
VERSION     WP_000998823.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Liu,X.
  TITLE     ABC Family Transporters
  JOURNAL   Adv Exp Med Biol 1141, 13-100 (2019)
   PUBMED   31571164
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Locher,K.P.
  TITLE     Mechanistic diversity in ATP-binding cassette (ABC) transporters
  JOURNAL   Nat Struct Mol Biol 23 (6), 487-493 (2016)
   PUBMED   27273632
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Theodoulou,F.L. and Kerr,I.D.
  TITLE     ABC transporter research: going strong 40 years on
  JOURNAL   Biochem Soc Trans 43 (5), 1033-1040 (2015)
   PUBMED   26517919
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Wilkens,S.
  TITLE     Structure and mechanism of ABC transporters
  JOURNAL   F1000Prime Rep 7, 14 (2015)
   PUBMED   25750732
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 256)
  AUTHORS   ter Beek,J., Guskov,A. and Slotboom,D.J.
  TITLE     Structural diversity of ABC transporters
  JOURNAL   J Gen Physiol 143 (4), 419-435 (2014)
   PUBMED   24638992
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Davidson,A.L., Dassa,E., Orelle,C. and Chen,J.
  TITLE     Structure, function, and evolution of bacterial ATP-binding
            cassette systems
  JOURNAL   Microbiol Mol Biol Rev 72 (2), 317-364 (2008)
   PUBMED   18535149
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Hollenstein,K., Dawson,R.J. and Locher,K.P.
  TITLE     Structure and mechanism of ABC transporter proteins
  JOURNAL   Curr Opin Struct Biol 17 (4), 412-418 (2007)
   PUBMED   17723295
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10004187
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..256
                     /product="ABC transporter permease"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_component="GO:0043190 - ATP-binding cassette (ABC)
                     transporter complex [Evidence IEA]"
                     /GO_function="GO:0042626 - ATPase-coupled transmembrane
                     transporter activity [Evidence IEA]"
                     /GO_function="GO:0140359 - ABC-type transporter activity
                     [Evidence IEA]"
                     /GO_process="GO:0055085 - transmembrane transport
                     [Evidence IEA]"
                     /calculated_mol_wt=29501
     Region          4..256
                     /region_name="TagG"
                     /note="ABC-type polysaccharide/teichoic acid/polyol
                     phosphate export permease [Carbohydrate transport and
                     metabolism]; COG1682"
                     /db_xref="CDD:441288"
ORIGIN      
        1 mndlkealar hqlwislgwn dvlgryrrsv lgpfwitism gvtisamgpl ygslfssgse
       61 nfimhltlgm ifwaflsati nescgifnes asiikqsdlp lylyilrvfy rqfmimlhnf
      121 iiipfvifft ntsvnldill fipaivitsi slistgmila ifctryrdmg pvvqsvvtlc
      181 ffitpiiwts eqlpkgrkef vdynifyyfm emlrkplmgt vpdvtiwfyt iitsiimlmv
      241 stlvltkyrs rivywl