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Database: UniProt
Entry: A0A158BYJ6_9BURK
LinkDB: A0A158BYJ6_9BURK
Original site: A0A158BYJ6_9BURK 
ID   A0A158BYJ6_9BURK        Unreviewed;       180 AA.
AC   A0A158BYJ6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Superoxide dismutase, Cu-Zn {ECO:0000313|EMBL:SAK75174.1};
GN   ORFNames=AWB75_04219 {ECO:0000313|EMBL:SAK75174.1};
OS   Caballeronia catudaia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK75174.1, ECO:0000313|Proteomes:UP000054870};
RN   [1] {ECO:0000313|EMBL:SAK75174.1, ECO:0000313|Proteomes:UP000054870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK75174.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FCOF02000020; SAK75174.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158BYJ6; -.
DR   OrthoDB; 5431326at2; -.
DR   Proteomes; UP000054870; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..178
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   180 AA;  18907 MW;  4C241A229105A156 CRC64;
     MRHGFDGRAA RTPGVLIALA ACSVMLSGCG LIFQNHEKRA DAVLQPTPGY AARGTVTLIE
     RADGVQVSYS VTDMPPNSDH ALTVHERGDC IAVNGQDSSP VFALPAERRK PGFRLEGELG
     NIHADATGAA TGFIVATDVS LDGVRSVISR AIMLHREAVD PYASAPHNVG PALACGVIRR
//
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