Y1797_DESRM
ID Y1797_DESRM Reviewed; 932 AA.
AC A4J5G9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=UPF0182 protein Dred_1797 {ECO:0000255|HAMAP-Rule:MF_01600};
GN OrderedLocusNames=Dred_1797;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01600};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01600}.
CC -!- SIMILARITY: Belongs to the UPF0182 family. {ECO:0000255|HAMAP-
CC Rule:MF_01600}.
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DR EMBL; CP000612; ABO50322.1; -; Genomic_DNA.
DR RefSeq; WP_011878134.1; NC_009253.1.
DR AlphaFoldDB; A4J5G9; -.
DR SMR; A4J5G9; -.
DR STRING; 349161.Dred_1797; -.
DR PRIDE; A4J5G9; -.
DR EnsemblBacteria; ABO50322; ABO50322; Dred_1797.
DR KEGG; drm:Dred_1797; -.
DR eggNOG; COG1615; Bacteria.
DR HOGENOM; CLU_007733_0_0_9; -.
DR OMA; HLRYPQD; -.
DR OrthoDB; 170146at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_01600; UPF0182; 1.
DR InterPro; IPR005372; UPF0182.
DR PANTHER; PTHR39344; PTHR39344; 1.
DR Pfam; PF03699; UPF0182; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..932
FT /note="UPF0182 protein Dred_1797"
FT /id="PRO_0000323476"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01600"
FT REGION 861..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 107068 MW; 53DCF816B9D38A86 CRC64;
MRGKSRFSLG LVILAGALLF SLIGWGAGLY IEWLWFKTLN YQQVFLTRLT SEIGLRVLVG
IIMFLLLLIN LMLTRKSVLK AVESAKAFRP FQRDDDNVIT INPNPQIDWR EQITPGRLTL
AFTLLSMALG FLYSSSVAGD WVTILQYFNQ SSFNITDPIF NKNLGFYFFS LPFWHIVYRI
LASAIFLNIV LVALVYLVTD TARGGLAKIF RFPSARYHLS VLAALFFVIK SWGYRLDQYD
LLYSSTGVVH GAGYTDIHAT LLAYKALMIL SLVTAIIIIA NIFLNRFRLT AYAIGGLLVT
SILLGSVYPA IIQKFVVLPN EFNREIPYIA NNIKFSQQAY NLDKIEQKDF PAGRTLQAKD
IQENKNTIDN IRLWDWQPLR QTYSQLQEMR LYYEFKNIDI DRYAIDEEYR QIMIAVREMN
QDQLPQQAKT WINQRLKYTH GYGIAMSPVN EVSGEGLPHF FLKDIPPVAS TNIKINRPEI
YYGESDDGYV IVNTKTDEFD YPKGDGNSYS KYEGDSGVKV NSFFRKLLFA FTFADYKLLF
TGDITNESQV LFYRNIKERI PKIAPFLSYD ADPYPVINNQ GEIYWMWDAY TISNMYPYSE
PFDDRGNNYI RNSVKVTMNA YNGSVNFYIS DAEDPIIKTY AKIFPGMFRP LSEMPEDLKK
HIRYPEDMFL VQSRMYSLYH MTDPQVFYNR EDKWTLPTEK VGEEEKAMDP YYTITVLPGE
KNPEYLLIMP FNPQNKKNMI AWLGARSDGE NYGKMVVYEF PKQELVYGPM QIEARIDQDT
TISQQLSLWD QRGSSVIRGN LLVIPVEDSL LYVEPLYLQS EQSKMPELRR VIVASGDKIV
MEPTLELALQ KIYGEGAVLK DRPQQGVPPA TDQPAGQQPA PEKTVKELAA EANRLYDDAQ
AKLKAGDWAG YGQSLNQLKD ILTKLQNQSF SQ