PHNC_RHIME
ID PHNC_RHIME Reviewed; 279 AA.
AC Q92V71; Q52906;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phosphonates import ATP-binding protein PhnC {ECO:0000255|HAMAP-Rule:MF_01713};
DE EC=7.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01713};
GN Name=phnC {ECO:0000255|HAMAP-Rule:MF_01713}; Synonyms=phoC;
GN OrderedLocusNames=RB0843; ORFNames=SMb21177;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2), and Plasmid pRmeSU47b.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=RCR2011 / SU47; PLASMID=pRmeSU47b;
RX PubMed=8755882; DOI=10.1128/jb.178.15.4540-4547.1996;
RA Bardin S., Dan S., Osteras M.T., Finan T.M.;
RT "A phosphate transport system is required for symbiotic nitrogen fixation
RT by Rhizobium meliloti.";
RL J. Bacteriol. 178:4540-4547(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021; PLASMID=pSymB (megaplasmid 2);
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Part of the ABC transporter complex PhnCDE involved in
CC phosphonates import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01713, ECO:0000269|PubMed:8755882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phosphonate(out) = ADP + H(+) + phosphate +
CC phosphonate(in); Xref=Rhea:RHEA:18065, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16215, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01713};
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:0000255|HAMAP-Rule:MF_01713}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01713}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01713}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphonates
CC importer (TC 3.A.1.9.1) family. {ECO:0000255|HAMAP-Rule:MF_01713}.
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DR EMBL; U59229; AAC44218.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49243.1; -; Genomic_DNA.
DR PIR; C95947; C95947.
DR RefSeq; NP_437383.1; NC_003078.1.
DR RefSeq; WP_010975699.1; NC_003078.1.
DR AlphaFoldDB; Q92V71; -.
DR SMR; Q92V71; -.
DR STRING; 266834.SM_b21177; -.
DR EnsemblBacteria; CAC49243; CAC49243; SM_b21177.
DR GeneID; 61600818; -.
DR KEGG; sme:SM_b21177; -.
DR PATRIC; fig|266834.11.peg.5774; -.
DR eggNOG; COG3638; Bacteria.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; MGRFPHV; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015416; F:ABC-type phosphonate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03256; ABC_PhnC_transporter; 1.
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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Phosphonate transport; Plasmid; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..279
FT /note="Phosphonates import ATP-binding protein PhnC"
FT /id="PRO_0000092725"
FT DOMAIN 2..245
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT CONFLICT 220
FT /note="H -> P (in Ref. 1; AAC44218)"
FT /evidence="ECO:0000305"
FT CONFLICT 265..279
FT /note="ETASAGLKPLALAGP -> KQHRPA (in Ref. 1; AAC44218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30044 MW; F38F647B4188AD6A CRC64;
MFQLKNVTRQ FGKKTAVSTV TFDIPQGQMV GIIGRSGAGK STLLRMINRL VDPSSGSIEF
AGLQVSSLKG AALRNWQRDC AMIFQQFNLV PRLDVLTNVL LGRLNHRSTV LSVLNMFSRE
ERIMAIGALE RLGIEQTALQ PAGTLSGGQQ QRVAIARALM QQPKVLLADE PIASLDPLNA
KIVMDALRDI NERDGITVIT NLHTLDTARN YCERVIGMAH GRVVFDGQPK DLTAAAVAAI
YGAETAIEES MTSTSINIPA EAPRETASAG LKPLALAGP
