ID A0A1M5BLV2_9BACT Unreviewed; 970 AA.
AC A0A1M5BLV2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative membrane-bound dehydrogenase domain-containing protein {ECO:0000313|EMBL:SHF43370.1};
GN ORFNames=SAMN05443144_108166 {ECO:0000313|EMBL:SHF43370.1};
OS Fodinibius roseus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Fodinibius.
OX NCBI_TaxID=1194090 {ECO:0000313|EMBL:SHF43370.1, ECO:0000313|Proteomes:UP000184041};
RN [1] {ECO:0000313|EMBL:SHF43370.1, ECO:0000313|Proteomes:UP000184041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21986 {ECO:0000313|EMBL:SHF43370.1,
RC ECO:0000313|Proteomes:UP000184041};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQUS01000008; SHF43370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5BLV2; -.
DR STRING; 1194090.SAMN05443144_108166; -.
DR OrthoDB; 9812332at2; -.
DR Proteomes; UP000184041; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd00920; Cupredoxin; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR013428; Membrane-bound_put_N.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
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 SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..142
FT /note="Blue (type 1) copper"
FT /evidence="ECO:0000259|Pfam:PF00127"
SQ SEQUENCE 970 AA; 108554 MW; D16A55EB33D9764B CRC64;
MKHFCEYACV YLYIIGAALI VTGFPAETAA QTSPSGEKQA METDRADRAY TLEAVITGYT
GIGGEIDGIR NPTLQARKGE TVRITIVNGE TLTHDIALEG MDVQSESIIE EGASTSVTFV
AESGDTYYCS IPGHRAAGME GRFEIISAST GETVAEGIIP QKDGQPVNLD FEYASLEGWS
AEGGAFTGQP VSDRSSELYE EDMDVDPSGQ FYVSSGGTKK AQATGTLTSP AFEVTHPWAA
FKVSGGALKE TRVEIVAAET DTTIFEITGN DHQRLRPVVV DLRGHRGQQI YIRLIDKETG
VSQIPYIEDN GWAHISFDDF RFYPERPRFR DELSPEDIVI LPPRDIIENA GLSGEEAVKE
MELPDPFSVT LAASEPDVVR PIAFTLDHRG RLWVAEAHTY PERAPEGEGK DRILIFEDTS
GDGKLDSRKV FIEGLNLVSG LEVGHGGVWV GAAPNLLYIP IDESGDSPAG EPEVLLNGWG
YQDTHETLNS FRWGPDGWLY GVQGVFTQSN VGKPGTPDDQ RQKINAGVWR YHPTRHEFEV
YARGTSNPWG LDFNAYGHPF ITACVIPHLF HVIQGARYRR QAGDHQNPHT YDDIKTIADH
VHWVGDQGPH AGNHRSGSAG GGHAHAGAMF YLGADHWPQE FRSTLFMNNI HGFRVNADKI
EREGSGYSAS HGKDFLKTHD SWSQWLDFRY SPGGSVWAID WYDKNQCHSP NPDVHNKTLG
RIYNIRHAED EHVRVNLKEK SSLELVEYQR HTNEWYVRHA RRILHERGPD ERVHEALRKM
LRGAPDITRK LRALWTLHVT EGLSDQEYID LLDHENEYLR SWALQLLGED NDIPERALKK
IARMAREEDS ALVRLYIASA LQRIAPAQRW SIVEGLYGHS EDADDHNLPL MIWYGTEPLV
TRDMERAAEM AMNTELPGIL TFTIRRIGAI GTPEARKLLK EVEGQLEQKP QSDRYDQARR
ELETIFGQAD
//
