DCTMQ_OLEA2
ID DCTMQ_OLEA2 Reviewed; 635 AA.
AC Q312S1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Isethionate TRAP transporter permease protein DctMQ {ECO:0000305|PubMed:30718429};
DE AltName: Full=TRAP transporter, fused DctMQ subunit {ECO:0000303|PubMed:30718429};
GN Name=dctMQ {ECO:0000303|PubMed:30718429};
GN OrderedLocusNames=Dde_1274 {ECO:0000312|EMBL:ABB38075.1};
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
RN [2]
RP FUNCTION, PATHWAY, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=30718429; DOI=10.1073/pnas.1815661116;
RA Peck S.C., Denger K., Burrichter A., Irwin S.M., Balskus E.P.,
RA Schleheck D.;
RT "A glycyl radical enzyme enables hydrogen sulfide production by the human
RT intestinal bacterium Bilophila wadsworthia.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:3171-3176(2019).
CC -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC transport system DctPQM involved in the uptake of isethionate (2-
CC hydroxyethanesulfonate), which is then catabolized by enzymes encoded
CC by adjacent genes in the locus. Thereby is involved in an anaerobic
CC respiration pathway that converts the sulfonate isethionate to ammonia,
CC acetate and sulfide. {ECO:0000269|PubMed:30718429}.
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000269|PubMed:30718429}.
CC -!- SUBUNIT: The complex comprises the periplasmic solute receptor protein
CC DctP, and the fused transmembrane protein DctMQ.
CC {ECO:0000305|PubMed:30718429}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC with isethionate as the terminal electron acceptor.
CC {ECO:0000269|PubMed:30718429}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAP transporter
CC small permease family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAP transporter
CC large permease family. {ECO:0000305}.
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DR EMBL; CP000112; ABB38075.1; -; Genomic_DNA.
DR AlphaFoldDB; Q312S1; -.
DR STRING; 207559.Dde_1274; -.
DR EnsemblBacteria; ABB38075; ABB38075; Dde_1274.
DR KEGG; dde:Dde_1274; -.
DR eggNOG; COG1593; Bacteria.
DR eggNOG; COG3090; Bacteria.
DR HOGENOM; CLU_019824_4_1_7; -.
DR OMA; TNIFVVC; -.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000002710; 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:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR010656; DctM.
DR InterPro; IPR004681; TRAP_DctM.
DR InterPro; IPR007387; TRAP_DctQ.
DR PANTHER; PTHR33362; PTHR33362; 1.
DR Pfam; PF06808; DctM; 1.
DR Pfam; PF04290; DctQ; 1.
DR TIGRFAMs; TIGR00786; dctM; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..635
FT /note="Isethionate TRAP transporter permease protein DctMQ"
FT /id="PRO_0000451053"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 67559 MW; 108A31046282B5D2 CRC64;
MSDPNVTATI MNAQGECSSG SLESRPGILG WLDANFEKPF LVAGMLAIIF IITFQTLYRY
IGVYLHEGAA AAVWTEEMAR FIFIWISYLA VPVAIKNRSS IRVDIIFDRL PVRFQNISWI
IVDVCFLTLA ATVLWQSLDL IKMQLTYPQT SPALQLPYYI PYLVLPVSFG LMAVRLLQDL
AGQVRICGAA DTVIGLILCA VLAAPLFIAD YIDPLPVLFG YFALFLVVGV PIAIGLGLAA
LATIVAAGSL PIDYVAQIAF TSIDSFPIMA IPFFIAAGVF MGAGGLSRRL LNLADEMLGA
LPGGMALATI GTCMFFAAIS GSGPATVAAI GSLTIPAMVE RGYCKYFSAA IVAAAGAIGV
MIPPSNPFVV YGVSAQASIG KLFMGGIVPG LLTGLALMAY SYWYSKKRGW KGEVRDRNLK
TFMHAVWEAK WALMVPVIVL GGIYGGIMTP TEAAALAAFY GLIIGCFVHR ELSCGSFYDC
VVEAAGTSAM VIVLMSMATI FGNIMTIEEV PTTIAQAMLG LTTDKIAILL MINVLLLIIG
TFMEALAAIV ILTPILLPIV LKVGVDPVHF GIIMVVNLAI GFVTPPVGVN LFVASGVANA
KIEQLSKVVL PLIALMLAVL LITTYVPAIP MFFAG
