PCAK_PSEPU
ID PCAK_PSEPU Reviewed; 448 AA.
AC Q51955;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=4-hydroxybenzoate transporter PcaK;
GN Name=pcaK;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PRS2000;
RX PubMed=7961399; DOI=10.1128/jb.176.21.6479-6488.1994;
RA Harwood C.S., Nichols N.N., Kim M.-K., Ditty J.L., Parales R.E.;
RT "Identification of the pcaRKF gene cluster from Pseudomonas putida:
RT involvement in chemotaxis, biodegradation, and transport of 4-
RT hydroxybenzoate.";
RL J. Bacteriol. 176:6479-6488(1994).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=PRS2000;
RX PubMed=9260946; DOI=10.1128/jb.179.16.5056-5061.1997;
RA Nichols N.N., Harwood C.S.;
RT "PcaK, a high-affinity permease for the aromatic compounds 4-
RT hydroxybenzoate and protocatechuate from Pseudomonas putida.";
RL J. Bacteriol. 179:5056-5061(1997).
RN [3]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF GLY-85; ASP-89; GLY-92 AND
RP ASP-323.
RC STRAIN=PRS2000;
RX PubMed=10438780; DOI=10.1128/jb.181.16.5068-5074.1999;
RA Ditty J.L., Harwood C.S.;
RT "Conserved cytoplasmic loops are important for both the transport and
RT chemotaxis functions of PcaK, a protein from Pseudomonas putida with 12
RT membrane-spanning regions.";
RL J. Bacteriol. 181:5068-5074(1999).
RN [4]
RP MUTAGENESIS OF ASP-41; ASP-44; ARG-124; GLU-144; HIS-183; HIS-328; ARG-386;
RP ARG-398 AND HIS-444.
RX PubMed=11844776; DOI=10.1128/jb.184.5.1444-1448.2002;
RA Ditty J.L., Harwood C.S.;
RT "Charged amino acids conserved in the aromatic acid/H+ symporter family of
RT permeases are required for 4-hydroxybenzoate transport by PcaK from
RT Pseudomonas putida.";
RL J. Bacteriol. 184:1444-1448(2002).
CC -!- FUNCTION: Transports 4-hydroxybenzoate (4-HBA) and protocatechuate
CC across the membrane. Driven by the proton motive force. Functions also
CC as a chemoreceptor, which is required for chemotaxis to aromatic acids.
CC {ECO:0000269|PubMed:7961399, ECO:0000269|PubMed:9260946}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 uM for 4-hydroxybenzoate {ECO:0000269|PubMed:9260946};
CC Vmax=25 nmol/min/mg enzyme with 4-hydroxybenzoate as substrate
CC {ECO:0000269|PubMed:9260946};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10438780,
CC ECO:0000269|PubMed:9260946}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10438780, ECO:0000269|PubMed:9260946}.
CC -!- DOMAIN: Amino acids located between the second and third, and the
CC eighth and ninth transmembrane regions are required for substrate
CC transport. {ECO:0000269|PubMed:10438780}.
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; U10895; AAA85137.1; -; Genomic_DNA.
DR RefSeq; WP_016498119.1; NZ_UGUX01000003.1.
DR AlphaFoldDB; Q51955; -.
DR SMR; Q51955; -.
DR STRING; 1240350.AMZE01000001_gene2837; -.
DR TCDB; 2.A.1.15.1; the major facilitator superfamily (mfs).
DR GeneID; 45522452; -.
DR eggNOG; COG2814; Bacteria.
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 GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
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; Chemotaxis; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..448
FT /note="4-hydroxybenzoate transporter PcaK"
FT /id="PRO_0000050321"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..67
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..119
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..184
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..301
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..421
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 41
FT /note="D->A,N: Abolishes 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 41
FT /note="D->E: Decrease in 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 44
FT /note="D->A,N: Abolishes 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 44
FT /note="D->E: Decrease in 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 85
FT /note="G->V: Abolishes 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 89
FT /note="D->N: Abolishes 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 92
FT /note="G->A: Decrease in 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 92
FT /note="G->C: No change in 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 92
FT /note="G->L,V: Abolishes 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 92
FT /note="G->Q: Decrease in 4-HBA transport and strong
FT decrease in chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 124
FT /note="R->A: Abolishes 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 144
FT /note="E->A: Strong decrease in 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 183
FT /note="H->A: Decrease in 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 323
FT /note="D->N: Abolishes 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:10438780"
FT MUTAGEN 328
FT /note="H->A: Decrease in 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 328
FT /note="H->R: Decrease in 4-HBA transport and loss of
FT chemotaxis."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 386
FT /note="R->A: Strong decrease in 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 398
FT /note="R->A: Abolishes 4-HBA transport."
FT /evidence="ECO:0000269|PubMed:11844776"
FT MUTAGEN 444
FT /note="H->A: No change in 4-HBA transport and chemotaxis."
FT /evidence="ECO:0000269|PubMed:11844776"
SQ SEQUENCE 448 AA; 47177 MW; 6D51C143123E99BC CRC64;
MNQAQNSVGK SLDVQSFINQ QPLSRYQWRV VLLCFLIVFL DGLDTAAMGF IAPALSQEWG
IDRASLGPVM SAALIGMVFG ALGSGPLADR FGRKGVLVGA VLVFGGFSLA SAYATNVDQL
LVLRFLTGLG LGAGMPNATT LLSEYTPERL KSLLVTSMFC GFNLGMAGGG FISAKMIPAY
GWHSLLVIGG VLPLLLALVL MVWLPESARF LVVRNRGTDK IRKTLSPIAP QVVAEAGSFS
VPEQKAVAAR SVFAVIFSGT YGLGTMLLWL TYFMGLVIVY LLTSWLPTLM RDSGASMEQA
AFIGALFQFG GVLSAVGVGW AMDRYNPHKV IGIFYLLAGV FAYAVGQSLG NITVLATLVL
IAGMCVNGAQ SAMPSLAARF YPTQGRATGV SWMLGIGRFG AILGAWSGAT LLGLGWNFEQ
VLTALLVPAA LATVGVIVKG LVSHADAT
