ID B2TML1_CLOBB Unreviewed; 466 AA.
AC B2TML1; U4P6I2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Amino acid carrier protein AlsT {ECO:0000313|EMBL:ACD24476.1};
GN OrderedLocusNames=CLL_A1000 {ECO:0000313|EMBL:ACD24476.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD24476.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363064};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363064}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the alanine or glycine:cation symporter (AGCS)
CC (TC 2.A.25) family. {ECO:0000256|ARBA:ARBA00009261,
CC ECO:0000256|RuleBase:RU363064}.
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DR EMBL; CP001056; ACD24476.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TML1; -.
DR KEGG; cbk:CLL_A1000; -.
DR PATRIC; fig|935198.13.peg.949; -.
DR HOGENOM; CLU_024867_0_1_9; -.
DR Proteomes; UP000001195; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; IEA:InterPro.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR001463; Na/Ala_symport.
DR NCBIfam; TIGR00835; agcS; 1.
DR PANTHER; PTHR30330; AGSS FAMILY TRANSPORTER, SODIUM-ALANINE; 1.
DR PANTHER; PTHR30330:SF1; AMINO-ACID CARRIER PROTEIN ALST; 1.
DR Pfam; PF01235; Na_Ala_symp; 1.
DR PRINTS; PR00175; NAALASMPORT.
DR PROSITE; PS00873; NA_ALANINE_SYMP; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU363064};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363064};
KW Symport {ECO:0000256|RuleBase:RU363064};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363064};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363064};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363064}.
FT TRANSMEM 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 82..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 178..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 342..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 381..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363064"
SQ SEQUENCE 466 AA; 50514 MW; E9A24B12459E076F CRC64;
MDILNNLLVA FNDFLYTYIL IALLIVLGLY FSYKTKFVQF RFIKEMFRLL GDGVTSERKK
GSVSSFQAFC ISTASRVGTG NLAGIAIAIS IGGPGAIFWM WIIALIGAGS SFVESTLAQI
YKTKDKNGAF RGGPAYYIEK GLNKKWMGVL FSILITVSFG LVFNSVQSNT ISLAMNEAFG
VNQITIGIIL TALTLVIIFG GVHRVAKVSE IIVPIMAVAY ILVSLFVVFK NFTHIPRVFT
LILENAFGLQ PAIGGTLGGT LMIGIKRGLF SNEAGMGSAP NAAATADVTH PVKQGLIQTL
GVFTDTIIIC SCTAFIILLA DIDLSGGLTG IQLTQNALSS QIGNFGTIFV AICILLFAFS
SIVGNYYYGE SNIEFLSKKK IYLIVYRIAV ASMVFFGSIA NLDIVWNLAD TFMGFMAIIN
LIAITLLGRF AFKALDDYRA QKKAGIKEPV FKASSIPELT NVDEWK
//
