LCOP_CORGL
ID LCOP_CORGL Reviewed; 630 AA.
AC Q8NN75; Q6M3B4;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Betaine/ectoine transporter LcoP {ECO:0000305};
DE AltName: Full=Low capacity osmoregulated permease {ECO:0000303|PubMed:15327991};
GN Name=lcoP {ECO:0000303|PubMed:15327991};
GN OrderedLocusNames=Cgl2334 {ECO:0000312|EMBL:BAB99727.1};
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 [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 [2]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15327991; DOI=10.1016/j.febslet.2004.07.067;
RA Steger R., Weinand M., Kraemer R., Morbach S.;
RT "LcoP, an osmoregulated betaine/ectoine uptake system from Corynebacterium
RT glutamicum.";
RL FEBS Lett. 573:155-160(2004).
RN [3]
RP ACTIVITY REGULATION, AND 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.
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 betaine and ectoine. Na(+) is probably the coupling ion.
CC {ECO:0000269|PubMed:15327991}.
CC -!- ACTIVITY REGULATION: Uptake is activated by hyperosmotic stress
CC (PubMed:15327991). Shows a small but significant chill stimulation
CC around 15 degrees Celsius (PubMed:15995189).
CC {ECO:0000269|PubMed:15327991, ECO:0000269|PubMed:15995189}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=154 uM for betaine {ECO:0000269|PubMed:15327991};
CC KM=539 uM for ectoine {ECO:0000269|PubMed:15327991};
CC KM=36 mM for Na(+) {ECO:0000269|PubMed:15327991};
CC Vmax=8.5 nmol/min/mg enzyme with betaine as substrate
CC {ECO:0000269|PubMed:15327991};
CC Vmax=8.6 nmol/min/mg enzyme with ectoine as substrate
CC {ECO:0000269|PubMed:15327991};
CC Temperature dependence:
CC Optimum temperature is 20 degrees Celsius (at low osmolality).
CC {ECO:0000269|PubMed:15995189};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression depends on the external osmolality
CC (PubMed:15327991). Induced upon hyperosmotic conditions, resulting in
CC an increase of its transport activity (PubMed:17390131).
CC {ECO:0000269|PubMed:15327991, ECO:0000269|PubMed:17390131}.
CC -!- SIMILARITY: Belongs to the BCCT transporter (TC 2.A.15) family.
CC {ECO:0000305}.
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DR EMBL; BA000036; BAB99727.1; -; Genomic_DNA.
DR RefSeq; NP_601534.1; NC_003450.3.
DR RefSeq; WP_011015047.1; NC_006958.1.
DR AlphaFoldDB; Q8NN75; -.
DR SMR; Q8NN75; -.
DR STRING; 196627.cg2563; -.
DR TCDB; 2.A.15.1.7; the betaine/carnitine/choline transporter (bcct) family.
DR KEGG; cgl:Cgl2334; -.
DR PATRIC; fig|196627.13.peg.2268; -.
DR eggNOG; COG1292; Bacteria.
DR HOGENOM; CLU_010118_4_0_11; -.
DR OMA; RVMSDIN; -.
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..630
FT /note="Betaine/ectoine transporter LcoP"
FT /id="PRO_0000441732"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 68320 MW; A29F2C5CD9B0E2ED CRC64;
MSTNSGNNLP ESQESPEEPH YPHDTHPGLV PGISVDAQRN KFGLDKTVFG VTAALILAFI
AWGISSPDSV SSVSSTMFSW AMTNTGWLLN FVMLIGIGTM LYIAFSRYGR IKLGTDEDEP
EFSRFSWIAM MFGAGIGVGI FFFGPSEPLW HYLSPPPHTV EGSTPESLHQ ALAQSHFHWG
LSAWGLYALV GGALAYSSYR RGRVTLISST FRSLFGEKTE GIAGRLIDMM AIIATLFGTA
ATLGLSAIQV GQGVQIISGA SEITNNILIA IIAILTIGFI ISSVSGVSKG IRYLSNLNIS
LTLGLVLFVF ITGPTLFLLN LIPSSVLEYG SEFLSMAGKS LSWGEETIEF QAGWTAFYWA
WWIAWTPFVG MFIARISRGR TLREFALITM AIPSFILILA FTIFGGTAIT MNRENVDGFD
GSSSKEQVLF DMFSNLPLYS ITPFILIFVL AVFFVTSADS ASVVMGTMSS QGNPAPNKLI
VVFWGLCMMG IAVVMLLTGG ESALTGLQNL TILIAIPFAL VLIVMAIAFI KDLSTDPAAI
RQRYAKAAIS NAVVRGLEEH GDDFELSIEP AEEGRGAGAT FDSTADHITD WYQRTDEEGN
DVDYDFTTGK WADGWTPEST EEGEVDAKKD
