BACH_NATPH
ID BACH_NATPH Reviewed; 291 AA.
AC P15647;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Halorhodopsin;
DE Short=HR;
DE AltName: Full=NpHR;
GN Name=hop;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=SP-1 / 28, and SP-1W;
RX PubMed=2104837; DOI=10.1016/s0021-9258(19)40006-9;
RA Lanyi J.K., Duschl A., Hatfield G.W., May K., Oesterhelt D.;
RT "The primary structure of a halorhodopsin from Natronobacterium pharaonis.
RT Structural, functional and evolutionary implications for bacterial
RT rhodopsins and halorhodopsins.";
RL J. Biol. Chem. 265:1253-1260(1990).
RN [2]
RP SPECTROPHOTOMETRIC STUDIES.
RC STRAIN=SP-1 / 28;
RX PubMed=8204571; DOI=10.1021/bi00187a002;
RA Scharf B., Engelhard M.;
RT "Blue halorhodopsin from Natronobacterium pharaonis: wavelength regulation
RT by anions.";
RL Biochemistry 33:6387-6393(1994).
CC -!- FUNCTION: Light-driven anion pump. Binding affinity for the anions is
CC in the order, bromide > chloride > nitrate > azide > bromate and
CC binding is pH dependent.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=~600 nm;
CC Note=In the presence of anions, the maximum absorption shifts to
CC about 577 nm.;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; J05199; AAA72222.1; -; Genomic_DNA.
DR PIR; A35002; A35002.
DR PDB; 3QBG; X-ray; 1.80 A; A/B/D=1-291.
DR PDB; 3QBI; X-ray; 2.10 A; A/B/D=1-291.
DR PDB; 3QBK; X-ray; 2.20 A; A/B/D=1-291.
DR PDB; 3QBL; X-ray; 2.20 A; A/B/D=1-291.
DR PDB; 3VVK; X-ray; 2.30 A; A/B/C/D/E/F=1-291.
DR PDBsum; 3QBG; -.
DR PDBsum; 3QBI; -.
DR PDBsum; 3QBK; -.
DR PDBsum; 3QBL; -.
DR PDBsum; 3VVK; -.
DR AlphaFoldDB; P15647; -.
DR SMR; P15647; -.
DR TCDB; 3.E.1.2.2; the ion-translocating microbial rhodopsin (mr) family.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR InterPro; IPR018229; Rhodopsin_retinal_BS.
DR PANTHER; PTHR28286; PTHR28286; 1.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR PRINTS; PR00251; BACTRLOPSIN.
DR SMART; SM01021; Bac_rhodopsin; 1.
DR PROSITE; PS00950; BACTERIAL_OPSIN_1; 1.
DR PROSITE; PS00327; BACTERIAL_OPSIN_RET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chromophore; Direct protein sequencing;
KW Ion transport; Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..291
FT /note="Halorhodopsin"
FT /id="PRO_0000196268"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 31..56
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..86
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 87..120
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 121..142
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 143..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 146..169
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 170..172
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..195
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 196..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 208..231
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 232..240
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 241..269
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 270..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 256
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 32..55
FT /evidence="ECO:0007829|PDB:3QBG"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 62..86
FT /evidence="ECO:0007829|PDB:3QBG"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:3QBG"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3QBG"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3QBG"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3QBL"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 122..141
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 146..168
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 173..195
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 208..231
FT /evidence="ECO:0007829|PDB:3QBG"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 241..255
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:3QBG"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:3QBG"
SQ SEQUENCE 291 AA; 31080 MW; 454832C666655FEA CRC64;
MTETLPPVTE SAVALQAEVT QRELFEFVLN DPLLASSLYI NIALAGLSIL LFVFMTRGLD
DPRAKLIAVS TILVPVVSIA SYTGLASGLT ISVLEMPAGH FAEGSSVMLG GEEVDGVVTM
WGRYLTWALS TPMILLALGL LAGSNATKLF TAITFDIAMC VTGLAAALTT SSHLMRWFWY
AISCACFLVV LYILLVEWAQ DAKAAGTADM FNTLKLLTVV MWLGYPIVWA LGVEGIAVLP
VGVTSWGYSF LDIVAKYIFA FLLLNYLTSN ESVVSGSILD VPSASGTPAD D
