PHND1_PROM0
ID PHND1_PROM0 Reviewed; 297 AA.
AC A3PC74;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Probable ABC transporter phosphite binding protein PhnD1 {ECO:0000305};
DE Flags: Precursor;
GN Name=phnD1 {ECO:0000303|PubMed:22011717};
GN OrderedLocusNames=P9301_07261 {ECO:0000312|EMBL:ABO17349.1};
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
RN [2]
RP FUNCTION AS A BINDING PROTEIN.
RC STRAIN=MIT 9301;
RX PubMed=22011717; DOI=10.1038/ismej.2011.149;
RA Feingersch R., Philosof A., Mejuch T., Glaser F., Alalouf O., Shoham Y.,
RA Beja O.;
RT "Potential for phosphite and phosphonate utilization by Prochlorococcus.";
RL ISME J. 6:827-834(2012).
CC -!- FUNCTION: Probably part of the ABC transporter complex PhnD1C1E1. Binds
CC strongly to inorganic phosphite and with very weak affinities to
CC methylphosphonate (MPn) and phosphate. {ECO:0000269|PubMed:22011717}.
CC -!- SUBUNIT: The complex may be composed of two ATP-binding proteins
CC (PhnC1), two transmembrane proteins (PhnE1) and a solute-binding
CC protein (PhnD1). {ECO:0000305|PubMed:22011717}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phosphate/phosphite/phosphonate binding
CC protein family. {ECO:0000305}.
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DR EMBL; CP000576; ABO17349.1; -; Genomic_DNA.
DR RefSeq; WP_011862714.1; NC_009091.1.
DR PDB; 5LQ5; X-ray; 1.46 A; A=25-297.
DR PDB; 5LQ8; X-ray; 1.52 A; A=25-297.
DR PDBsum; 5LQ5; -.
DR PDBsum; 5LQ8; -.
DR AlphaFoldDB; A3PC74; -.
DR SMR; A3PC74; -.
DR STRING; 167546.P9301_07261; -.
DR EnsemblBacteria; ABO17349; ABO17349; P9301_07261.
DR KEGG; pmg:P9301_07261; -.
DR eggNOG; COG3221; Bacteria.
DR HOGENOM; CLU_051472_6_2_3; -.
DR OMA; QVQLAWF; -.
DR Proteomes; UP000001430; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR030836; ABC_peri_PhnD-like.
DR InterPro; IPR005770; PhnD.
DR TIGRFAMs; TIGR01098; 3A0109s03R; 1.
DR TIGRFAMs; TIGR04553; ABC_peri_selen; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..297
FT /note="Probable ABC transporter phosphite binding protein
FT PhnD1"
FT /id="PRO_5002656325"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 39..57
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5LQ5"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5LQ5"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:5LQ5"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:5LQ5"
SQ SEQUENCE 297 AA; 33809 MW; 565A83178722586C CRC64;
MFNLKYFLVS SSLLFSVFSS PVFSNPKVLK VGAIPDQNQD VLDKRFNLFS KELSKQLDVE
VKYIPVINYI AAVTGFRTKD LDLVWFGGLS GVQARLQTPN SIVIAQRDID KEFKSVFVVN
KNLELNSISN IKGLKKLKNL RFTFGSENST SGRLMPEYFL NQAGVEIKHF KGKKAGFSGS
HDATIALVNS GAFDAGALNK QVWENNLKNN PKRTSNLELF WITPEYVDYH WVAQGDLENR
FGEGFTKELK SVILNLDIKQ KSHKQILDMF NAKRFIKAES KQYKNIEEIG RKLNKIR
