ID A0A127FD28_STEDE Unreviewed; 153 AA.
AC A0A127FD28;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Azurin {ECO:0000256|RuleBase:RU363017};
GN ORFNames=ACG33_14605 {ECO:0000313|EMBL:AMN48307.1};
OS Steroidobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Steroidobacterales;
OC Steroidobacteraceae; Steroidobacter.
OX NCBI_TaxID=465721 {ECO:0000313|EMBL:AMN48307.1, ECO:0000313|Proteomes:UP000070250};
RN [1] {ECO:0000313|EMBL:AMN48307.1, ECO:0000313|Proteomes:UP000070250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18526 {ECO:0000313|EMBL:AMN48307.1,
RC ECO:0000313|Proteomes:UP000070250};
RA Yang F.-C., Chen Y.-L., Yu C.-P., Tang S.-L., Wang P.-H., Ismail W.,
RA Wang C.-H., Yang C.-Y., Chiang Y.-R.;
RT "A Comprehensive Approach to Explore the Metabolic and Phylogenetic
RT Diversity of Bacterial Steroid Degradation in the Environment: Testosterone
RT as an Example.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers electrons from cytochrome c551 to cytochrome
CC oxidase. {ECO:0000256|RuleBase:RU363017}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU363017}.
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DR EMBL; CP011971; AMN48307.1; -; Genomic_DNA.
DR RefSeq; WP_066922279.1; NZ_CP011971.1.
DR AlphaFoldDB; A0A127FD28; -.
DR STRING; 465721.ACG33_14605; -.
DR KEGG; sdf:ACG33_14605; -.
DR PATRIC; fig|465721.4.peg.3124; -.
DR OrthoDB; 9814063at2; -.
DR Proteomes; UP000070250; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd13922; Azurin; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR014068; Azurin.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR008972; Cupredoxin.
DR NCBIfam; TIGR02695; azurin; 1.
DR PANTHER; PTHR38439; AURACYANIN-B; 1.
DR PANTHER; PTHR38439:SF2; OUTER MEMBRANE PROTEIN H.8; 1.
DR Pfam; PF00127; Copper-bind; 1.
DR SUPFAM; SSF49503; Cupredoxins; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU363017};
KW Electron transport {ECO:0000256|RuleBase:RU363017};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363017}; Periplasm {ECO:0000256|RuleBase:RU363017};
KW Reference proteome {ECO:0000313|Proteomes:UP000070250};
KW Signal {ECO:0000256|RuleBase:RU363017};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363017}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU363017"
FT CHAIN 26..153
FT /note="Azurin"
FT /evidence="ECO:0000256|RuleBase:RU363017"
FT /id="PRO_5007356342"
FT DOMAIN 27..151
FT /note="Blue (type 1) copper"
FT /evidence="ECO:0000259|Pfam:PF00127"
SQ SEQUENCE 153 AA; 16003 MW; 91DD0A90ED8FB444 CRC64;
MLNSRSARIA IAASLLTAVS SMAMAKTCDV TIEGDDRMKF DKAEIAVAAD CTEVNLTLKH
AGKLPVAAMG HNWVLTETSA FQAVATAGAS AGPAANYVPK GDARVLAHTK LVGGGESTSI
KFSTAALKKG GDYTFFCSFP GHWAVMKGKF KFE
//
