ECTP_CORGL
ID ECTP_CORGL Reviewed; 615 AA.
AC Q79VE0; H7C678; O86143;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ectoine/glycine betaine/proline transporter EctP {ECO:0000305};
GN Name=ectP {ECO:0000303|PubMed:9811661};
GN OrderedLocusNames=Cgl2312 {ECO:0000312|EMBL:BAB99705.1};
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, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND INDUCTION.
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 BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15995189; DOI=10.1128/jb.187.14.4752-4759.2005;
RA Ozcan N., Kraemer R., Morbach S.;
RT "Chill activation of compatible solute transporters in Corynebacterium
RT glutamicum at the level of transport activity.";
RL J. Bacteriol. 187:4752-4759(2005).
RN [4]
RP INDUCTION, AND SUBCELLULAR LOCATION.
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, proline and glycine betaine. Na(+) is probably the coupling
CC ion. {ECO:0000269|PubMed:9811661}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for ectoine {ECO:0000269|PubMed:9811661};
CC KM=333 uM for glycine betaine {ECO:0000269|PubMed:9811661};
CC KM=1200 uM for proline {ECO:0000269|PubMed:9811661};
CC KM=9100 uM for Na(+) {ECO:0000269|PubMed:9811661};
CC Vmax=27 nmol/min/mg enzyme with ectoine as substrate
CC {ECO:0000269|PubMed:9811661};
CC Vmax=34 nmol/min/mg enzyme with glycine betaine as substrate
CC {ECO:0000269|PubMed:9811661};
CC Vmax=34 nmol/min/mg enzyme with proline as substrate
CC {ECO:0000269|PubMed:9811661};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius (irrespective of the state
CC of osmotic stimulation). {ECO:0000269|PubMed:15995189};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17390131};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Constitutively expressed (PubMed:9811661). Induced upon
CC hyperosmotic conditions, but the already high maximal uptake capacity
CC is not further elevated, indicating that the amount of EctP is not
CC changed (PubMed:17390131). {ECO:0000269|PubMed:17390131,
CC ECO:0000269|PubMed:9811661}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
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DR EMBL; AJ001436; CAA04760.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99705.1; -; Genomic_DNA.
DR RefSeq; NP_601511.1; NC_003450.3.
DR RefSeq; WP_011015032.1; NC_006958.1.
DR AlphaFoldDB; Q79VE0; -.
DR SMR; Q79VE0; -.
DR STRING; 196627.cg2539; -.
DR TCDB; 2.A.15.1.2; the betaine/carnitine/choline transporter (bcct) family.
DR KEGG; cgl:Cgl2312; -.
DR PATRIC; fig|1718.43.peg.2262; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_4_1_11; -.
DR OMA; QAMQIAF; -.
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 GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR000060; BCCT_transptr.
DR PANTHER; PTHR30047; PTHR30047; 1.
DR Pfam; PF02028; BCCT; 1.
DR TIGRFAMs; TIGR00842; bcct; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Stress response; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="Ectoine/glycine betaine/proline transporter EctP"
FT /id="PRO_0000441731"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 524..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 67403 MW; 832D85A58CA14FE7 CRC64;
MSSNIAITTE PEGKNKKGLK SDPFIFSISV GFIVVFVIAT IALGEKARTT FSAIAGWLLE
NLGWMYIGGV SLVFIFLMGI FASRYGRVKL GDDDDDPEHT LIVWFCMLFA GGVGAVLMFW
GVAEPINHAF NVPMANEESM SEAAIVQAFA YTFYHFGIHM WVIMALPGLS LGYFIYKRKL
PPRLSSVFSP ILGKHIYSTP GKLIDVLAIV GTTFGIAVSV GLGVLQINAG MNKLWSTPQV
SWVQLLIILI ITAVACISVA SGLDKGIKLL SNINIAMAVA LMFFILFTGP TLTLLRFLVE
SFGIYASWMP NLMFWTDSFQ DNPGWQGKWT VFYWAWTICW SPYVGMFVAR ISRGRTVREF
IGGVLALPAI FGVVWFSIFG RAGIEVELSN PGFLTQPTVV EGDVPAALFN VLQEYPLTGI
VSAFALVIIV IFFITSIDSA ALVNDMFATG AENQTPTSYR VMWACTIGAV AGSLLIISPS
SGIATLQEVV IIVAFPFFLV QFVMMFSLLK GMSEDAAAVR RVQTRQWEKT DTPEKLEEHS
SQPAPGYDDE GNPLPMPALE HDEDGNIVIP GNVVIEGDLG VVGDVVDDPE EAQEMGSRFK
IVEQTRPQSR DEYDI
