PHNC2_HALMA
ID PHNC2_HALMA Reviewed; 271 AA.
AC Q5UW69;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Phosphonates import ATP-binding protein PhnC 2 {ECO:0000255|HAMAP-Rule:MF_01713};
DE EC=7.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01713};
GN Name=phnC2 {ECO:0000255|HAMAP-Rule:MF_01713}; OrderedLocusNames=rrnB0320;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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}.
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 membrane {ECO:0000255|HAMAP-Rule:MF_01713};
CC Peripheral membrane protein {ECO:0000255|HAMAP-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; AY596298; AAV48484.1; -; Genomic_DNA.
DR RefSeq; WP_004966649.1; NZ_CP039136.1.
DR AlphaFoldDB; Q5UW69; -.
DR SMR; Q5UW69; -.
DR STRING; 272569.rrnB0320; -.
DR EnsemblBacteria; AAV48484; AAV48484; rrnB0320.
DR GeneID; 40150957; -.
DR GeneID; 64824603; -.
DR KEGG; hma:rrnB0320; -.
DR PATRIC; fig|272569.17.peg.4313; -.
DR eggNOG; arCOG00206; Archaea.
DR HOGENOM; CLU_000604_1_22_2; -.
DR OMA; LWAHRTV; -.
DR Proteomes; UP000001169; Chromosome II.
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 membrane; Membrane; Nucleotide-binding;
KW Phosphonate transport; Reference proteome; Translocase; Transport.
FT CHAIN 1..271
FT /note="Phosphonates import ATP-binding protein PhnC 2"
FT /id="PRO_0000092742"
FT DOMAIN 2..246
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
FT REGION 243..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01713"
SQ SEQUENCE 271 AA; 29804 MW; 3AF8CCD50A87E789 CRC64;
MLTVDNLEKT YDSGDRALKG VSFEVSGNEI VAIIGPSGAG KSTLVRSINR LTEPTGGRIS
LDDTEVTGLE KSALRDVRRD MGMIFQEFNL VERLTVMENI LSGRLGYLST WNAFRRNFPP
EDIRRAREIL SRVNLEGVEN NRADELSGGQ RQRVGIARAV IQRPKILLAD EPTSALDPDT
SREVMSLLTD IAHEDDIPII INIHEVDLAV DYADRIIGLS DGEIVFNGPP DDLDQAARDE
IYRGGESIAD REEPSAGNST DADDVIAERG D