PHND2_PROM0
ID PHND2_PROM0 Reviewed; 292 AA.
AC A3PDP9;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Probable ABC transporter phosphonate/phosphite binding protein PhnD2 {ECO:0000305};
DE Flags: Precursor;
GN Name=phnD2 {ECO:0000303|PubMed:22011717};
GN OrderedLocusNames=P9301_12511 {ECO:0000312|EMBL:ABO17874.1};
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 PhnC2D2E2. Binds
CC strongly to methylphosphonate (MPn), ethylphosphonate (EPn) and
CC inorganic phosphite. {ECO:0000269|PubMed:22011717}.
CC -!- SUBUNIT: The complex may be composed of two ATP-binding proteins
CC (PhnC2), two transmembrane proteins (PhnE2) and a solute-binding
CC protein (PhnD2). {ECO:0000305|PubMed:22011717}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the phosphate/phosphite/phosphonate binding
CC protein family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000576; ABO17874.1; -; Genomic_DNA.
DR RefSeq; WP_011863200.1; NC_009091.1.
DR PDB; 5LV1; X-ray; 2.12 A; A/B/C=22-292.
DR PDBsum; 5LV1; -.
DR AlphaFoldDB; A3PDP9; -.
DR SMR; A3PDP9; -.
DR STRING; 167546.P9301_12511; -.
DR EnsemblBacteria; ABO17874; ABO17874; P9301_12511.
DR KEGG; pmg:P9301_12511; -.
DR eggNOG; COG3221; Bacteria.
DR HOGENOM; CLU_051472_6_4_3; -.
DR OMA; YIYPSLW; -.
DR Proteomes; UP000001430; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR InterPro; IPR005770; PhnD.
DR TIGRFAMs; TIGR01098; 3A0109s03R; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..292
FT /note="Probable ABC transporter phosphonate/phosphite
FT binding protein PhnD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5002656612"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5LV1"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5LV1"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5LV1"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5LV1"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:5LV1"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:5LV1"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:5LV1"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:5LV1"
SQ SEQUENCE 292 AA; 31304 MW; 99F19364615C06F8 CRC64;
MKLKSLLSVF TISIVALTSA CSTKNAGPSA DPDKLIVALI PDENAATVIQ DNQGLKDYLT
EAFDKEIELV VTTDYSSMIE AARNDRLDLA YFGPLSYVLA KAVSDIEPFA ARIKGGTKTY
NSCIIGNTKK GVTSFDDIKG TTFALGDPAS TSSRLFPELT LAENGLTKGK DFQGVFLGSH
DAVALAVQNG NAQAGGMACP ILKSLKKKGV IDPSKVTTIA QSSPIPQYPW TMRSTLSPEL
KEKIRFTFLD LDSDKVLKPF NADGFASITD SDYDGIRKAG KLLGLDLSKF VK
