ID   PHND_MYCS2              Reviewed;         321 AA.
AC   A0QQ71; I7FDW7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Phosphate-import protein PhnD;
DE   Flags: Precursor;
GN   Name=phnD; OrderedLocusNames=MSMEG_0649, MSMEI_0632;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   INVOLVEMENT IN PHOSPHATE ASSIMILATION, AND GENE NAME.
RX   PubMed=15758213; DOI=10.1099/mic.0.27624-0;
RA   Tran S.L., Rao M., Simmers C., Gebhard S., Olsson K., Cook G.M.;
RT   "Mutants of Mycobacterium smegmatis unable to grow at acidic pH in the
RT   presence of the protonophore carbonyl cyanide m-chlorophenylhydrazone.";
RL   Microbiology 151:665-672(2005).
RN   [5]
RP   FUNCTION IN PHOSPHATE TRANSPORT, AND INDUCTION.
RX   PubMed=17074913; DOI=10.1099/mic.0.29201-0;
RA   Gebhard S., Tran S.L., Cook G.M.;
RT   "The Phn system of Mycobacterium smegmatis: a second high-affinity ABC-
RT   transporter for phosphate.";
RL   Microbiology 152:3453-3465(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex PhnCDE involved in
CC       phosphate import. Responsible for phosphate binding.
CC       {ECO:0000269|PubMed:17074913}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PhnC),
CC       two transmembrane proteins (PhnE) and a solute-binding protein (PhnD).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: By phosphate-limited conditions, via derepression by PhnF,
CC       and probably also via the two-component regulatory system senX3/regX3.
CC       {ECO:0000269|PubMed:17074913}.
CC   -!- SIMILARITY: Belongs to the phosphate/phosphite/phosphonate binding
CC       protein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AFP37113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK73977.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37113.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003892069.1; NZ_SIJM01000009.1.
DR   RefSeq; YP_885059.1; NC_008596.1.
DR   AlphaFoldDB; A0QQ71; -.
DR   SMR; A0QQ71; -.
DR   STRING; 246196.MSMEI_0632; -.
DR   TCDB; 3.A.1.9.2; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; ABK73977; ABK73977; MSMEG_0649.
DR   EnsemblBacteria; AFP37113; AFP37113; MSMEI_0632.
DR   GeneID; 66738826; -.
DR   KEGG; msg:MSMEI_0632; -.
DR   KEGG; msm:MSMEG_0649; -.
DR   PATRIC; fig|246196.19.peg.645; -.
DR   eggNOG; COG3221; Bacteria.
DR   OMA; QGMRFDK; -.
DR   OrthoDB; 988224at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
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   Cell membrane; Lipoprotein; Membrane; Palmitate; Phosphate transport;
KW   Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..321
FT                   /note="Phosphate-import protein PhnD"
FT                   /id="PRO_0000357470"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   321 AA;  33385 MW;  B4B1D2809903748D CRC64;
     MKIRAHHKIA TAAACVALLA SACSGSDKPQ STTAEGFPET ITLAAIPAEN SSDLKASYDP
     LIKMLEKQTG SKVEFVQASD YAGVVEGMIA GNVDLAFFGP FAYVVAGVNG AKMTPLGAVI
     KDEGGAPGYQ SYGLARADED NINGLKDFAG KKVCFVDPGS TSGFLYPTAG LIEEGVVKSG
     SEADISAAMS PIFAGGHDSS ALAIANGDCD AGFAFDTMVD KTMIDKGDLK PGQLKTVWKS
     DMIAGSVFAA NDALGPEVID KLKTMFAQDA NVKSFEEEGF CEGDACRITD ERAWGVVPVT
     DADYDGVRHV CDVTGSEKCK G