PHNC_MYCS2
ID PHNC_MYCS2 Reviewed; 263 AA.
AC A0QQ70; I7FWR1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphate-import ATP-binding protein PhnC;
DE EC=7.3.2.1;
GN Name=phnC; OrderedLocusNames=MSMEG_0647, MSMEI_0631;
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 energy coupling to the transport
CC system. {ECO:0000269|PubMed:17074913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in);
CC Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.1;
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:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
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 ABC transporter superfamily.
CC Phosphonate/phosphate importer (TC 3.A.1.9.2) family. {ECO:0000305}.
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DR EMBL; CP000480; ABK73331.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37112.1; -; Genomic_DNA.
DR RefSeq; WP_011727093.1; NZ_SIJM01000009.1.
DR RefSeq; YP_885058.1; NC_008596.1.
DR AlphaFoldDB; A0QQ70; -.
DR SMR; A0QQ70; -.
DR STRING; 246196.MSMEI_0631; -.
DR TCDB; 3.A.1.9.2; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ABK73331; ABK73331; MSMEG_0647.
DR EnsemblBacteria; AFP37112; AFP37112; MSMEI_0631.
DR GeneID; 66738825; -.
DR KEGG; msg:MSMEI_0631; -.
DR KEGG; msm:MSMEG_0647; -.
DR PATRIC; fig|246196.19.peg.644; -.
DR eggNOG; COG3638; Bacteria.
DR OMA; GWAHRLV; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015416; F:ABC-type phosphonate transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015415; F:ATPase-coupled phosphate ion transmembrane transporter activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR012693; ABC_transpr_PhnC.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02315; ABC_phnC; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51249; PHNC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Phosphate transport; Reference proteome; Translocase; Transport.
FT CHAIN 1..263
FT /note="Phosphate-import ATP-binding protein PhnC"
FT /id="PRO_0000357468"
FT DOMAIN 11..254
FT /note="ABC transporter"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 263 AA; 28585 MW; 7FBE2420568AE13A CRC64;
MNPVAGDDVV VIARDVTKRF GDTLALDHVS LDVHRSELLV LLGLSGSGKS TLLRCLNGLH
PVTSGTVDVG GTRVDQASGA QLRALRRRVG FVFQHFNLVG RLSCLENVLI GGLGRLRLPR
YGALTYPRHM RAEALAHLDR VGLADYADRR ADTLSGGQQQ RVAIARTLMQ KPALLLADEP
VASLDPENAG VVMDLLFRVC IEEKLTVVCT LHQVDLALGW AHRLVGLQGG RKVLDRPAVG
MTRDDVMAVY QRVEPAVTPA RRV