BACR1_HALMA
ID BACR1_HALMA Reviewed; 250 AA.
AC Q5UXY6;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Bacteriorhodopsin-I;
DE Short=HmBRI;
GN Name=bop; OrderedLocusNames=rrnAC3161;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2]
RP FUNCTION, INDUCTION, CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20802037; DOI=10.1128/jb.00642-10;
RA Fu H.Y., Lin Y.C., Chang Y.N., Tseng H., Huang C.C., Liu K.C., Huang C.S.,
RA Su C.W., Weng R.R., Lee Y.Y., Ng W.V., Yang C.S.;
RT "A novel six-rhodopsin system in a single archaeon.";
RL J. Bacteriol. 192:5866-5873(2010).
CC -!- FUNCTION: Light-driven proton pump. {ECO:0000269|PubMed:20802037}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=552 nm {ECO:0000269|PubMed:20802037};
CC Note=10 nm blue-shift for lambda max in pH=9.0.;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expressed constitutively throughout the growth phases, both
CC in presence and absence of white light. {ECO:0000269|PubMed:20802037}.
CC -!- PTM: The covalent binding of retinal to the apoprotein, bacterioopsin,
CC generates bacteriorhodopsin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; AY596297; AAV47867.1; -; Genomic_DNA.
DR PDB; 4PXK; X-ray; 2.50 A; A=1-250.
DR PDB; 7DOH; X-ray; 1.45 A; I=242-250.
DR PDBsum; 4PXK; -.
DR PDBsum; 7DOH; -.
DR AlphaFoldDB; Q5UXY6; -.
DR SMR; Q5UXY6; -.
DR STRING; 272569.rrnAC3161; -.
DR TCDB; 3.E.1.1.5; the ion-translocating microbial rhodopsin (mr) family.
DR EnsemblBacteria; AAV47867; AAV47867; rrnAC3161.
DR KEGG; hma:rrnAC3161; -.
DR PATRIC; fig|272569.17.peg.3701; -.
DR eggNOG; arCOG02812; Archaea.
DR HOGENOM; CLU_054785_5_1_2; -.
DR OMA; MFLGMLY; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Chromophore; Hydrogen ion transport; Ion transport; Membrane;
KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..250
FT /note="Bacteriorhodopsin-I"
FT /id="PRO_0000428849"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 83
FT /note="Primary proton acceptor"
FT /evidence="ECO:0000250"
FT MOD_RES 220
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT HELIX 8..29
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 35..59
FT /evidence="ECO:0007829|PDB:4PXK"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:4PXK"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:4PXK"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 79..98
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 103..125
FT /evidence="ECO:0007829|PDB:4PXK"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 134..158
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 169..195
FT /evidence="ECO:0007829|PDB:4PXK"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 205..227
FT /evidence="ECO:0007829|PDB:4PXK"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:4PXK"
SQ SEQUENCE 250 AA; 26946 MW; 2B7D1909189C477F CRC64;
MPAPGSEGIW LWLGTAGMFL GMLYFIARGW GETDGRRQKF YIATILITAI AFVNYLAMAL
GFGLTFIEFG GEQHPIYWAR YTDWLFTTPL LLYDLGLLAG ADRNTIYSLV SLDVLMIGTG
VVATLSAGSG VLSAGAERLV WWGISTAFLL VLLYFLFSSL SGRVANLPSD TRSTFKTLRN
LVTVVWLVYP VWWLVGSEGL GLVGIGIETA GFMVIDLVAK VGFGIILLRS HGVLDGAAET
TGTGATPADD
