ID B1XZ28_LEPCP Unreviewed; 581 AA.
AC B1XZ28;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=TRAP dicarboxylate transporter, DctM subunit {ECO:0000313|EMBL:ACB34047.1};
DE Flags: Precursor;
GN OrderedLocusNames=Lcho_1780 {ECO:0000313|EMBL:ACB34047.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB34047.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB34047.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system. {ECO:0000256|RuleBase:RU369079}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|RuleBase:RU369079}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|RuleBase:RU369079}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001013; ACB34047.1; -; Genomic_DNA.
DR AlphaFoldDB; B1XZ28; -.
DR STRING; 395495.Lcho_1780; -.
DR KEGG; lch:Lcho_1780; -.
DR eggNOG; COG4664; Bacteria.
DR HOGENOM; CLU_019824_3_0_4; -.
DR OrthoDB; 9796052at2; -.
DR Proteomes; UP000001693; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR010656; DctM.
DR InterPro; IPR004681; TRAP_DctM.
DR PANTHER; PTHR33362; SIALIC ACID TRAP TRANSPORTER PERMEASE PROTEIN SIAT-RELATED; 1.
DR PANTHER; PTHR33362:SF7; SLL1103 PROTEIN; 1.
DR Pfam; PF06808; DctM; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|RuleBase:RU369079};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU369079}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..513
FT /note="TRAP C4-dicarboxylate transport system permease DctM
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF06808"
FT REGION 537..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 62068 MW; 3C8BC27A87F54C51 CRC64;
MIEFLSANMA PIMFMGLIVF LLMGYSVAFS LGACGLVFGF IGIELGLLPA ALIQALPLRI
FGIMQNDTLL AIPFFTFMGL ILERSGMAED LLDTIGQLFG PIRGGLAYAV IFVGAMLAAT
TGVVAASVIS MGLISLPIML RYGYDRRIAS GVIAASGTLA QIIPPSLVLI IMADQLGQSV
GDLYKGAFIP GFVLTGLYVG YIALISLWKP TWVPALPKEA RTIREDNGDS GLPSLGVLVL
LSTALAVAFA KTRPDTTPTD ELIVVSMCVG VGVAFLLSVI NKAIGLKLLS KMAERVTFVL
IPPLALIFLV LGTIFLGIAT PTEGGAMGAV GALLMALGRR RLDMKLLRQA MDSTMKLATF
VVFILVGSTV FSLSFQGVDG PKWVEHLLTG LPGGQVGFLI VVNILIFVLA FFLDFFELSF
IVVPLLGPVA AALGIDLVWF GVLLAVNMQT SFMHPPFGFA LFYLRSVAPN KDYKDRLTGQ
MIPKVTTGQI YWGAVPFVVI QVIMVGLLIA FPDLVSGGLG KKEAINIDDV QIEFQTQETA
PEVDPNSMFE KSANNPGGSG EAKEPDPMDA FKDLPKDEEK K
//
