PROP_CORGL
ID PROP_CORGL Reviewed; 504 AA.
AC Q79VC4; H7C6A8; O69284;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ectoine/proline transporter ProP {ECO:0000305};
GN Name=proP {ECO:0000303|PubMed:9811661};
GN OrderedLocusNames=Cgl3066 {ECO:0000312|EMBL:BAC00460.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=9811661; DOI=10.1128/jb.180.22.6005-6012.1998;
RA Peter H., Weil B., Burkovski A., Kramer R., Morbach S.;
RT "Corynebacterium glutamicum is equipped with four secondary carriers for
RT compatible solutes: identification, sequencing, and characterization of the
RT proline/ectoine uptake system, ProP, and the ectoine/proline/glycine
RT betaine carrier, EctP.";
RL J. Bacteriol. 180:6005-6012(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP ACTIVITY REGULATION.
RX PubMed=16239220; DOI=10.1074/jbc.m508362200;
RA Tsatskis Y., Khambati J., Dobson M., Bogdanov M., Dowhan W., Wood J.M.;
RT "The osmotic activation of transporter ProP is tuned by both its C-terminal
RT coiled-coil and osmotically induced changes in phospholipid composition.";
RL J. Biol. Chem. 280:41387-41394(2005).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=17390131; DOI=10.1007/s00253-007-0938-4;
RA Weinand M., Kraemer R., Morbach S.;
RT "Characterization of compatible solute transporter multiplicity in
RT Corynebacterium glutamicum.";
RL Appl. Microbiol. Biotechnol. 76:701-708(2007).
CC -!- FUNCTION: Involved in the uptake of osmoprotectants. Can transport
CC ectoine and proline. Protons are probably the coupling ions.
CC {ECO:0000269|PubMed:9811661}.
CC -!- ACTIVITY REGULATION: Uptake is activated by osmotic stress
CC (PubMed:16239220). Inhibited by CCCP (PubMed:9811661).
CC {ECO:0000269|PubMed:16239220, ECO:0000269|PubMed:9811661}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48 uM for proline {ECO:0000269|PubMed:9811661};
CC KM=132 uM for ectoine {ECO:0000269|PubMed:9811661};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced upon hyperosmotic conditions, resulting in an
CC increase of its transport activity. {ECO:0000269|PubMed:17390131}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y12537; CAA73136.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00460.1; -; Genomic_DNA.
DR RefSeq; NP_602258.1; NC_003450.3.
DR RefSeq; WP_011015605.1; NC_006958.1.
DR AlphaFoldDB; Q79VC4; -.
DR SMR; Q79VC4; -.
DR STRING; 196627.cg3395; -.
DR KEGG; cgl:Cgl3066; -.
DR PATRIC; fig|196627.13.peg.2998; -.
DR eggNOG; COG0477; Bacteria.
DR HOGENOM; CLU_001265_39_0_11; -.
DR OMA; PLNRQDY; -.
DR Proteomes; UP000000582; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Stress response; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..504
FT /note="Ectoine/proline transporter ProP"
FT /id="PRO_0000441733"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 477..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 54276 MW; CC550C2671B6B4F4 CRC64;
MSPIRSKKKI KNEPRLTVDD VNVVPPKKIR PAIKGTVVGN FMEWYDFGIY GYLTVTMTAV
FTQGLPQEWQ LLAVMFGFAV SYLVRPLGGL VLGPLGDKVG RQKVLYVTMA MMAVSTALIG
LLPTAASIGA WALVLLYLLK MVQGFSTGGE YAGATTYVAE FAPDRRRGFF GAFLDMGSYL
GFAAGASVVA ITTWVTTHFY GATAMEDFGW RIPFLTAIPL GIIAVYLRTR IPETPAFENN
QDEPNAVVEK DTEDPYARLG LAGVIRHHWR PLLIGIAIVA ATNTAGYALT SYMPVYLEEQ
IGLHSASAAA VTVPILVVMS LLLPFVGMWS DRVGRKPVYA TAVAATLILM VPAFLIMNTG
TIGAVLIALS MVAIPTGLYV ALSASALPAL FPTASRFSGM GISYNISVSL FGGTTPLITQ
FLLQKTGLDI VPALYIMFFS AIAGVALLFM TESSQKPLLG SFPTVETKSE AVEIVKNQDE
DPNIDLSHMP FPDEENVGAE KQNA