MULTISPECIES: heme/hemoglobin uptake receptor PhuR [Pseudomonas].

LOCUS       WP_003113453             764 aa            linear   BCT 31-MAY-2021
ACCESSION   WP_003113453
VERSION     WP_003113453.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Smith,A.D., Modi,A.R., Sun,S., Dawson,J.H. and Wilks,A.
  TITLE     Spectroscopic Determination of Distinct Heme Ligands in
            Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa
  JOURNAL   Biochemistry 54 (16), 2601-2612 (2015)
   PUBMED   25849630
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Smith,A.D. and Wilks,A.
  TITLE     Differential contributions of the outer membrane receptors PhuR and
            HasR to heme acquisition in Pseudomonas aeruginosa
  JOURNAL   J Biol Chem 290 (12), 7756-7766 (2015)
   PUBMED   25616666
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  :: BlastRule
            Evidence Accession :: NBR013163
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..764
                     /gene="phuR"
     Protein         1..764
                     /product="heme/hemoglobin uptake receptor PhuR"
                     /calculated_mol_wt=84594
     Region          44..762
                     /region_name="OM_channels"
                     /note="Porin superfamily. These outer membrane channels
                     share a beta-barrel structure that differ in strand and
                     shear number. Classical (gram-negative) porins are
                     non-specific channels for small hydrophillic molecules and
                     form 16 beta-stranded barrels (16,20)...; cl21487"
                     /db_xref="CDD:473880"
     Site            order(51..60,70..79,92..97,104..111,130..140,152..160)
                     /site_type="active"
                     /note="N-terminal plug [active]"
                     /db_xref="CDD:238657"
     Site            order(336,359)
                     /site_type="other"
                     /note="ligand-binding site [chemical binding]"
                     /db_xref="CDD:238657"
ORIGIN      
        1 mplsppfalr pclallllsp slalagnavp ltpttitatr teqavdsvps tvsvqtreql
       61 drqnvnnike lvryepgvsv ggagqragit gynirgidgn riltqidgve lpndffsgpy
      121 aqthrnyvdp divkrveilr gpasalygsn aiggavsyft ldpsdiikdg kdvgarlkag
      181 yesashswlt satvagradd fdgllhygyr qghetesngg hggtglsrse anpedadsys
      241 llgklgwnya egsrfglvfe kyksdvdtdq ksayggpydk gkpaippsml pggmyqwrkg
      301 ndtltreryg lehhflldsq vadriqwsln yqlaktdqat refyypitrk vlrtrdttyk
      361 erlwvfdsql dksfaigete hllsyginlk hqkvtgmrsg tgtnldtgad sprdalerss
      421 dfpdptvkty alfaqdsisw ndwtftpglr ydytrmephi tdeflrtmkq sqntavdesd
      481 kkwhrvspkf gvtydfaqhy twygqyaqgf rtptakalyg rfenlqagyh iepnpnlkpe
      541 ksqsfetglr gkfdegsfgv avfynkyrdf idedalntds tggngqtfqs nnieravikg
      601 velkgrlelg afgapqglyt qgsvayaygr nkdngepins vnpltgvfgl gydeadgnyg
      661 gllswtlvkr kdrvddstfh tpdgtasqfk tpgfgvldls ayyrlskdlt lnaglynltd
      721 kkywlwddvr gydsvgeasa lapanidrls qpgrnfavnl vwdi