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Database: UniProt
Entry: I0K6M0_9BACT
LinkDB: I0K6M0_9BACT
Original site: I0K6M0_9BACT 
ID   I0K6M0_9BACT            Unreviewed;      1279 AA.
AC   I0K6M0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Membrane-bound dehydrogenase domain protein {ECO:0000313|EMBL:CCG99773.1};
GN   ORFNames=FAES_1763 {ECO:0000313|EMBL:CCG99773.1};
OS   Fibrella aestuarina BUZ 2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG99773.1, ECO:0000313|Proteomes:UP000011058};
RN   [1] {ECO:0000313|EMBL:CCG99773.1, ECO:0000313|Proteomes:UP000011058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX   PubMed=22689241; DOI=10.1128/JB.00550-12;
RA   Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT   "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT   Bacterium.";
RL   J. Bacteriol. 194:3555-3555(2012).
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DR   EMBL; HE796683; CCG99773.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0K6M0; -.
DR   STRING; 1166018.FAES_1763; -.
DR   KEGG; fae:FAES_1763; -.
DR   PATRIC; fig|1166018.3.peg.3500; -.
DR   eggNOG; COG1413; Bacteria.
DR   eggNOG; COG2133; Bacteria.
DR   eggNOG; COG3241; Bacteria.
DR   eggNOG; COG3828; Bacteria.
DR   HOGENOM; CLU_274839_0_0_10; -.
DR   Proteomes; UP000011058; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   CDD; cd04233; Auracyanin; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013428; Membrane-bound_put_N.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR   InterPro; IPR029010; ThuA-like.
DR   NCBIfam; TIGR02604; Piru_Ver_Nterm; 1.
DR   PANTHER; PTHR33546; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   PANTHER; PTHR33546:SF1; LARGE, MULTIFUNCTIONAL SECRETED PROTEIN-RELATED; 1.
DR   Pfam; PF00127; Copper-bind; 1.
DR   Pfam; PF06283; ThuA; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011058}.
FT   DOMAIN          58..258
FT                   /note="ThuA-like"
FT                   /evidence="ECO:0000259|Pfam:PF06283"
FT   DOMAIN          1152..1270
FT                   /note="Blue (type 1) copper"
FT                   /evidence="ECO:0000259|Pfam:PF00127"
FT   REGION          872..909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1279 AA;  140399 MW;  BE14C885ADA6B935 CRC64;
     MTTSMNRALL VTALVTLALT NCRRTPTQVM RDVDGKTTTS KATRQAGPRR TEILFLGDNG
     HHRPAERVPQ LMAALGNRGI NITYTDQLND LNADNLSKYD GLLIFANWDS IPKPQEQALL
     DFVASGKGLI PVHCASFCFR NSAEYVDKVV GGQFWRHRMD TIQTRTVDAN SEIMAGLPPI
     KAFDETYLHT HLQPDNHVLA VRDIKADQAK DKPGQKEEPY TWTRTYGKGR VFYTAYGHDE
     RTWSQPGFQQ LLERGILWSV GDAVKKQHDD LKPQAFAYKE AQLPNYEKRP GVQLEQLPLS
     PDESMKHIQV PADFSLSLFA HEPNVMHPIA MTWDDRGRLY VLITKDYPNE RKPEGGSDSI
     VMCEDTNGDG KADKFTNYAD GLSIPTGMVW ANGGLIVSQA PHMLFLRDTN GDDRVDEKKI
     LFTGFGTFDT HAGPSNLHYG FDNWIWGSVG YSGFKGKGTA DKDSLQFGQA LFRFRPDGSH
     VEFMTGTSNN TWGMGFNETG DVFGSTANNS HGWYMAIPNR SYNARQGSVP GGRSTDTHKD
     MKPITEKVRQ VDVFGGFTAA AGHNFYTARA FPKAYWNEIA FVSEPTGHIV HMNRMKRTGT
     DYEDVEPTAG QGFNLMAGAD EWFAPVFAQV GPDGAVWVAD WYSYIIQHNP VPQGFKNGSG
     NAYETDLRDF THGRIYRVGY NKAPAETQKI VSLNPNDPAG LVAALSNSNQ FWRMKAQRLL
     VERGNKDVVP QLWAVANNPT VDEIGINAPA IHALWTLHGL GAITPSDLEK ALKHPCAHVR
     KTAVQVMPRD AAGANMLLAR NTLNDGEPLV VLQSLLALSE APVTPAIDEA VLTRLRQTTA
     NDDRWLPDAF ACALNRNGAA LLRQWLSSIK ESGGTHTQQH DHSAMAHNQS SASGQMASTQ
     SGPASVVSTN TPKVDGIDLV IDRVAMQPTS PLVREGARTT IYVRNQGSVA VPKGTAVPLS
     MRFQAKDAAN KQKIDYVSYT FTDGIAPGET VGINRVNNGP WVGDLSLSGE RAGDYTLTIT
     IDKDQKLSES NVRNNTHTAT LTVKAPAQLK TVALERAARA YASTASPDSI AAMLTKATTL
     GEDNANALVK GLSEGYDYRQ RRKATPATGT LLASVAEGIP ADARPRMNRL LEAWGLRDAN
     ADLDPNAQIV RLKTVREEMR FDQTSFTVKA GKQVVIVLEN PDAMQHNLVV GKPKSLERIG
     KLADDMITAK DGAERNYVPT TPDVLAATAL VNPSQTVRLT FKAPDQPGEY PYLCTFPGHW
     RLMKGIMKVE KEGTASAAK
//
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