ID A0A0J5GE64_9NEIS Unreviewed; 462 AA.
AC A0A0J5GE64;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Copper oxidase {ECO:0000313|EMBL:KMJ52789.1};
GN ORFNames=ACG97_11515 {ECO:0000313|EMBL:KMJ52789.1};
OS Vogesella sp. EB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ52789.1, ECO:0000313|Proteomes:UP000054352};
RN [1] {ECO:0000313|EMBL:KMJ52789.1, ECO:0000313|Proteomes:UP000054352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB {ECO:0000313|EMBL:KMJ52789.1,
RC ECO:0000313|Proteomes:UP000054352};
RA Arrua Day P., Revale S., Alvarez H.M.;
RT "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT Vogesella sp. strain EB.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004459}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004459}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMJ52789.1}.
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DR EMBL; LFDT01000019; KMJ52789.1; -; Genomic_DNA.
DR RefSeq; WP_047967513.1; NZ_LFDT01000019.1.
DR AlphaFoldDB; A0A0J5GE64; -.
DR STRING; 1526735.ACG97_11515; -.
DR PATRIC; fig|1526735.3.peg.2459; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000054352; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13860; CuRO_1_2dMco_1; 1.
DR CDD; cd04202; CuRO_D2_2dMcoN_like; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054352};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..462
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005261394"
FT DOMAIN 88..194
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 220..335
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 436..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50946 MW; 336860423ABBB074 CRC64;
MSIDQSRRQF FAGAATAVVG ATVARSALAA LPEAVIQTSV ETAPPLLPES GRPYNPVVTL
NGWTLPWRMN NGVKEFHLVA EPVEREMAPG FTAQLWGYNG QSPGPTIEVV EGDRVRIFVT
NKLPEHTSIH WHGQRLPNGM DGVSGLTQRS IKPGKTFVYG FVARRPGTFM YHPHADEMVQ
MAMGMHGFWV THPKGKHPLI DEVDRDFCFL LNAFDVEPGS KTPKVNTMTD FNIWAWNSRI
FPGIDSLNVR LNDKVRIRVG NLTMTNHPIH LHGHEFLVTG TDGGPTPRST RWHEVTTDVA
VGQMRQLEFV ADEEGDWAIH CHKSHHTMNA MGHDVPTMIG VDHRGLVGKI QQVAPDYMLM
GERGMADMGE MEMPIPDNTA PMMTGQGPFG PLEMGGMFSV LKVRKDQPAG NYKDPGWFRH
PAGTVAYEYN GELPAASRQP AAANPAAATV KAKKPGTHPE QH
//
