ID C0N3B7_9GAMM Unreviewed; 597 AA.
AC C0N3B7;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Copper-resistance protein, CopA family {ECO:0000313|EMBL:EEF80655.1};
GN ORFNames=MDMS009_594 {ECO:0000313|EMBL:EEF80655.1};
OS Methylophaga thiooxydans DMS010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF80655.1, ECO:0000313|Proteomes:UP000004679};
RN [1] {ECO:0000313|EMBL:EEF80655.1, ECO:0000313|Proteomes:UP000004679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF80655.1,
RC ECO:0000313|Proteomes:UP000004679};
RX PubMed=21478352; DOI=10.1128/JB.00388-11;
RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., Schafer H.;
RT "Draft genome sequence of the chemolithoheterotrophic, halophilic
RT methylotroph Methylophaga thiooxydans DMS010.";
RL J. Bacteriol. 193:3154-3155(2011).
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DR EMBL; GG657889; EEF80655.1; -; Genomic_DNA.
DR RefSeq; WP_008290361.1; NZ_GG657889.1.
DR AlphaFoldDB; C0N3B7; -.
DR HOGENOM; CLU_009100_5_2_6; -.
DR OrthoDB; 9757546at2; -.
DR Proteomes; UP000004679; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13874; CuRO_2_CopA; 1.
DR CDD; cd13896; CuRO_3_CopA; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR006376; Cu-R_CopA.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034282; CuRO_2_CopA.
DR InterPro; IPR034279; CuRO_3_CopA.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01480; copper_res_A; 1.
DR PANTHER; PTHR11709:SF218; FI03373P-RELATED; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
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:UP000004679};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002900972"
FT DOMAIN 57..165
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 209..336
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 479..596
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 597 AA; 66647 MW; FC4945720C489D1E CRC64;
MAKTLPSSRR KFIKSALGLS SALVLARLAP VWASPLGRSY GELIHSDGPI DLLIEQSPMN
VAGKSAFPIT LNGSMPGPLI RLREGQRAQL NVTNALKTDT SIHWHGIILP ENMDGVPGVS
FPGIKPGETF HYEFDVTQNG TYWYHSHSGL QEQVGHLGPL VIEPADGDIG ADREHVILLS
DWTFEDPHAV YRNLKVAEGY YNYQQRTLSD TFDDIKKQGL ADTWKQRSMW NKMRMSSRDI
LDVTGSFYTY LMNGRDSETN WTALYRPGEK IRLRIINGSA MSFFDFRIPG LEMVVVAADG
QPVKPVTVDE FRIGVAETYD VIVQPKDSQP YTFFAESIDR SGYVRGTLAT EMGQQAEVPE
LRPTPERGMD AMGMGMDHDM GSMGATNMDS MAMSHKGHEM ASGSMDGMQH QEHAISATRP
IAPVIDIKHT KAGHGPGAAM LAENPTSRLN EPGIGLENVN HRVLVYGDLI GAHPWPDERE
PERQIELHLT GNMERYMWSF DGVKFSEVDG PVEFHHGERL RLVLVNDTMM DHPIHLHGMW
MELENGQYPR PRKHTISLKP SEVVSLQISA DAPGSWAFHC HLLYHMKAGM FRVVSVV
//
