HCY_NATPH
ID HCY_NATPH Reviewed; 163 AA.
AC P39442; Q9UWL3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Halocyanin;
DE Flags: Precursor;
GN Name=hcy;
OS Natronomonas pharaonis (Natronobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=2257;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, LIPIDATION AT
RP CYS-25, ACETYLATION AT CYS-25, AND MASS SPECTROMETRY.
RC STRAIN=SP-1 / 28;
RX PubMed=8195126; DOI=10.1016/s0021-9258(17)36556-0;
RA Mattar S., Scharf B., Kent S.B.H., Rodewald K., Oesterhelt D.,
RA Engelhard M.;
RT "The primary structure of halocyanin, an archaeal blue copper protein,
RT predicts a lipid anchor for membrane fixation.";
RL J. Biol. Chem. 269:14939-14945(1994).
RN [2]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 144-163.
RX PubMed=8251512; DOI=10.1021/bi00210a043;
RA Scharf B., Engelhard M.;
RT "Halocyanin, an archaebacterial blue copper protein (type I) from
RT Natronobacterium pharaonis.";
RL Biochemistry 32:12894-12900(1993).
CC -!- FUNCTION: Electron donor. Binds one copper ion.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +183 mV.;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC -!- MASS SPECTROMETRY: Mass=15456; Mass_error=1.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8195126};
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DR EMBL; Z30236; CAA82942.1; -; Genomic_DNA.
DR PIR; A53792; A53792.
DR AlphaFoldDB; P39442; -.
DR SMR; P39442; -.
DR iPTMnet; P39442; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR017533; Halocyanin.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF00127; Copper-bind; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR03102; halo_cynanin; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Copper; Direct protein sequencing;
KW Electron transport; Lipoprotein; Membrane; Metal-binding; Signal;
KW Transport.
FT SIGNAL 1..24
FT CHAIN 25..163
FT /note="Halocyanin"
FT /id="PRO_0000002871"
FT DOMAIN 48..163
FT /note="Plastocyanin-like"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="N-acetylcysteine"
FT /evidence="ECO:0000269|PubMed:8195126"
FT LIPID 25
FT /note="S-archaeol cysteine"
FT /evidence="ECO:0000269|PubMed:8195126"
SQ SEQUENCE 163 AA; 17222 MW; DB180417F8B0BEE6 CRC64;
MKDISRRRFV LGTGATVAAA TLAGCNGNGN GNGNGNGNGE PDTPEGRADQ FLTDNDALMY
DGDITDETGQ DEVVVVTGAG NNGFAFDPAA IRVDVGTTVT WEWTGDGGAH NVVSEPESDF
EFESDRVDEE GFTFEQTFDD EGVALYVCTP HRAQGMYGAV IVE
