ID A4G290_HERAR Unreviewed; 213 AA.
AC A4G290;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Protein DedA {ECO:0000313|EMBL:CAL60627.1};
GN Name=dedA {ECO:0000313|EMBL:CAL60627.1};
GN OrderedLocusNames=HEAR0407 {ECO:0000313|EMBL:CAL60627.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60627.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL60627.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367016};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU367016}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DedA family. {ECO:0000256|ARBA:ARBA00010792,
CC ECO:0000256|RuleBase:RU367016}.
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DR EMBL; CU207211; CAL60627.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G290; -.
DR STRING; 204773.HEAR0407; -.
DR KEGG; har:HEAR0407; -.
DR eggNOG; COG0586; Bacteria.
DR HOGENOM; CLU_044208_6_1_4; -.
DR OrthoDB; 9813426at2; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR032818; DedA.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR30353; INNER MEMBRANE PROTEIN DEDA-RELATED; 1.
DR PANTHER; PTHR30353:SF0; TRANSMEMBRANE PROTEIN; 1.
DR Pfam; PF09335; SNARE_assoc; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367016};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367016};
KW Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367016};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367016}.
FT TRANSMEM 21..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367016"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367016"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367016"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367016"
FT DOMAIN 48..172
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
SQ SEQUENCE 213 AA; 23773 MW; 9CAF6152A495B0A0 CRC64;
MDFMQFFDMI LHVDKYLGTF IAQYGALIYL VLFTIIFCET GLVVFPFLPG DTLLFIAGAF
CASGGMNLWL LLSLLIVAAI LGNTVNYWIG QRIGEKVFTH DYRWLDRAAL QKTHSFYENH
GGKTLILARF LPIVRTFAPF VAGVSKMTFV RFQFFNVTGA VLWVALLVVG GYLFGNIPII
RDHLNTIVLV GVGAAAIPVA LGALWKLAQR FKK
//