ID   AZUP_PARPN              Reviewed;         145 AA.
AC   P80401;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Pseudoazurin;
DE   Flags: Precursor;
GN   Name=pazS;
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=82367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-32.
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC   82005 / GB17;
RX   PubMed=9032456; DOI=10.1042/bj3210699;
RA   Leung Y.-C., Chan C., Reader J.S., Willis A.C., van Spanning R.J.M.,
RA   Ferguson S.J., Radford S.E.;
RT   "The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream
RT   putative regulatory sequences and overexpression in Escherichia coli.";
RL   Biochem. J. 321:699-705(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-145.
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC   82005 / GB17;
RX   PubMed=7772045; DOI=10.1042/bj3080585;
RA   Chan C., Willis A.C., Robinson C.V., Aplin R.T., Radford S.E.,
RA   Ferguson S.J.;
RT   "The complete amino acid sequence confirms the presence of pseudoazurin in
RT   Thiosphaera pantotropha.";
RL   Biochem. J. 308:585-590(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA   Williams P.A.;
RL   Submitted (FEB-1997) to the PDB data bank.
CC   -!- FUNCTION: This soluble electron transfer copper protein is required for
CC       the inactivation of copper-containing nitrite reductase in the presence
CC       of oxygen.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC       Note=Binds 1 copper ion per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
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DR   EMBL; Z73141; CAA97485.1; -; mRNA.
DR   EMBL; Z70033; CAA93848.1; -; Genomic_DNA.
DR   PIR; S55326; S55326.
DR   RefSeq; WP_024842647.1; NZ_RIAQ01000021.1.
DR   PDB; 1ADW; X-ray; 2.50 A; A/B=23-145.
DR   PDB; 3ERX; X-ray; 1.25 A; A/B=23-145.
DR   PDB; 4BWT; X-ray; 1.76 A; A/B=23-145.
DR   PDB; 4BWU; X-ray; 1.76 A; A/B=23-145.
DR   PDB; 4BXV; X-ray; 1.76 A; A/B=23-145.
DR   PDBsum; 1ADW; -.
DR   PDBsum; 3ERX; -.
DR   PDBsum; 4BWT; -.
DR   PDBsum; 4BWU; -.
DR   PDBsum; 4BXV; -.
DR   AlphaFoldDB; P80401; -.
DR   BMRB; P80401; -.
DR   SMR; P80401; -.
DR   STRING; 935565.JAEM01000002_gene3605; -.
DR   eggNOG; COG3794; Bacteria.
DR   EvolutionaryTrace; P80401; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   CDD; cd04218; Pseudoazurin; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002386; Amicyanin/Pseudoazurin.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR028871; BlueCu_1_BS.
DR   InterPro; IPR001235; Copper_blue_Plastocyanin.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR012745; Pseudoazurin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00155; AMICYANIN.
DR   PRINTS; PR00156; COPPERBLUE.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   TIGRFAMs; TIGR02375; pseudoazurin; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Electron transport;
KW   Metal-binding; Periplasm; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:7772045,
FT                   ECO:0000269|PubMed:9032456"
FT   CHAIN           23..145
FT                   /note="Pseudoazurin"
FT                   /id="PRO_0000002850"
FT   DOMAIN          27..115
FT                   /note="Plastocyanin-like"
FT   REGION          126..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   STRAND          24..33
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   STRAND          36..47
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   STRAND          51..59
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   TURN            104..107
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   STRAND          109..117
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   HELIX           121..126
FT                   /evidence="ECO:0007829|PDB:3ERX"
FT   HELIX           131..141
FT                   /evidence="ECO:0007829|PDB:3ERX"
SQ   SEQUENCE   145 AA;  15446 MW;  725ECB5929EC3831 CRC64;
     MFHHSLAAAA AALLALAAPG FAATHEVHML NKGESGAMVF EPAFVRAEPG DVINFVPTDK
     SHNVEAIKEI LPEGVESFKS KINESYTLTV TEPGLYGVKC TPHFGMGMVG LVQVGDAPEN
     LDAAKTAKMP KKARERMDAE LAQVN