ID A0A0Q5ZC54_9BURK Unreviewed; 473 AA.
AC A0A0Q5ZC54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Copper oxidase {ECO:0000313|EMBL:KQT11545.1};
GN ORFNames=ASG30_06660 {ECO:0000313|EMBL:KQT11545.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT11545.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT11545.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT11545.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT11545.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT11545.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:KQT11545.1}.
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DR EMBL; LMQL01000009; KQT11545.1; -; Genomic_DNA.
DR RefSeq; WP_055895686.1; NZ_LMQL01000009.1.
DR AlphaFoldDB; A0A0Q5ZC54; -.
DR STRING; 1736365.ASG30_06660; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000051173; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; 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; 2.
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:UP000051173}.
FT DOMAIN 92..197
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 225..337
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 433..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52126 MW; 134CFD5F922CBBBE CRC64;
MTEHNRRSFL TGVGAIAGAV SAATVGKVAM AALPEPVIQT LPDTAGPLAP KTGRPYNPVV
TLNGWTLPWR MNNGVKEYHL VAEPVVREMA PGFKAHLWGY NGQSPGPTIE VVEGDRVRIF
VTNRLPEHTS IHWHGQRLPN GMDGVSGLTQ KAIPAGKTFV YEFVARRPGT FMYHPHADEM
TQMAMGMMGF WVTHPKARTP LIEEVDRDFV FLLSAYDVEP GSYTPRIMTM LDFNLWTFNS
RIFPGIDSMN VRRGDKVRIR FGNLTMTNHP IHIHGHEFTV TGTDGGPTPR STRWKEVTTD
VAVGQMRQVE FLADEEGDWA FHCHKSHHTM NAMGHGVPTM IGVDHRDVAR KIGRLVPDYM
VMGERGMADM GEMEMPLPDN TAPMMTGQGP FGGLEMGGMF TTVKVRHDQK PGDYGDPGWF
RHPPGTVAYE FTGQLPEPAR ARSPARPAAG AAPSKDVEVR VRKPSGSSGH GAH
//
