PCAK_ACIAD
ID PCAK_ACIAD Reviewed; 457 AA.
AC Q43975; Q6FBL1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=4-hydroxybenzoate transporter PcaK {ECO:0000303|PubMed:24907408};
DE Short=4-HB transporter {ECO:0000305};
GN Name=pcaK {ECO:0000303|PubMed:8063101}; OrderedLocusNames=ACIAD1709;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8063101; DOI=10.1016/0378-1119(94)90829-x;
RA Kowalchuk G.A., Hartnett G.B., Benson A., Houghton J.E., Ngai K.-L.,
RA Ornston L.N.;
RT "Contrasting patterns of evolutionary divergence within the Acinetobacter
RT calcoaceticus pca operon.";
RL Gene 146:23-30(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=24907408; DOI=10.1016/j.pep.2014.05.011;
RA Pernstich C., Senior L., MacInnes K.A., Forsaith M., Curnow P.;
RT "Expression, purification and reconstitution of the 4-hydroxybenzoate
RT transporter PcaK from Acinetobacter sp. ADP1.";
RL Protein Expr. Purif. 101:68-75(2014).
CC -!- FUNCTION: Uptake of 4-hydroxybenzoate (4-HB). Can also transport a
CC variety of aromatic acids with hydroxyl substitutions at the 2-, 3- and
CC 4-positions, such as salicylate, 2,4-dihydroxybenzoate,
CC protocatechuate, 3-hydroxybenzoate, vanillate and gentisate.
CC {ECO:0000269|PubMed:24907408}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:24907408}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:24907408}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Aromatic
CC acid:H(+) symporter (AAHS) (TC 2.A.1.15) family. {ECO:0000305}.
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DR EMBL; L05770; AAC37151.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG68551.1; -; Genomic_DNA.
DR AlphaFoldDB; Q43975; -.
DR SMR; Q43975; -.
DR STRING; 62977.ACIAD1709; -.
DR EnsemblBacteria; CAG68551; CAG68551; ACIAD1709.
DR KEGG; aci:ACIAD1709; -.
DR eggNOG; COG2271; Bacteria.
DR HOGENOM; CLU_001265_46_4_6; -.
DR OMA; AGMCVNG; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR004746; MFS_AAHS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00895; 2A0115; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..457
FT /note="4-hydroxybenzoate transporter PcaK"
FT /id="PRO_0000050320"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..72
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..128
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..191
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..310
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..363
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..426
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24907408"
FT CONFLICT 439
FT /note="A -> R (in Ref. 1; AAC37151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 49192 MW; 4F5B40ADA61A1567 CRC64;
MPKEANMASQ DYATQRSSLD AQALINDAPL SRYQWLIAIV CFLIVFVDGI DTAAMGFIAP
ALAQDWGVDR SQLGPVMSAA LGGMIIGALV SGPTADRFGR KIVLSMSMLV FGGFTLACAY
STNLDSLVIF RFLTGIGLGA AMPNATTLFS EYCPARIRSL LVTCMFCGYN LGMAIGGFIS
SWLIPAFGWH SLFLLGGWAP LILMLLVIFF LPESYRFLIV KGKNTKKVRQ ILSRIAPQKV
QGVTEFHVPE EKVEAGTKKG VFGMLFSAKY VKGTVLLWVT YFMGLVMIYL LTSWLPTLMR
ETGASLERAA FLGGLFQFGG VLSALFIGWA MDRFNPNRII AGFYLAAGIF AVIVGQSLSN
PTLLALFILC AGIAVNGAQS SMPVLSARFY PTQCRATGVA WMSGIGRFGA VFGAWIGAVL
LGNNWSFTMI LSMLIIPAAA AAIAIFVKSL VAHTDAT
