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BACH_HALMA
ID   BACH_HALMA              Reviewed;         276 AA.
AC   Q5V1N0;
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=Halorhodopsin;
DE            Short=HmHR;
DE   Flags: Precursor;
GN   Name=hop; OrderedLocusNames=rrnAC1659;
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 chloride pump. {ECO:0000269|PubMed:20802037}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=576 nm {ECO:0000269|PubMed:20802037};
CC         Note=If the chloride concentration decreases, the spectrum exhibits a
CC         red-shift.;
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; AAV46572.1; -; Genomic_DNA.
DR   RefSeq; WP_011223771.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V1N0; -.
DR   SMR; Q5V1N0; -.
DR   STRING; 272569.rrnAC1659; -.
DR   EnsemblBacteria; AAV46572; AAV46572; rrnAC1659.
DR   GeneID; 40152624; -.
DR   KEGG; hma:rrnAC1659; -.
DR   PATRIC; fig|272569.17.peg.2347; -.
DR   eggNOG; arCOG02811; Archaea.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   OMA; VCRQVFW; -.
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   Chromophore; Ion transport; Membrane; Photoreceptor protein;
KW   Pyrrolidone carboxylic acid; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..20
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000428851"
FT   CHAIN           21..276
FT                   /note="Halorhodopsin"
FT                   /id="PRO_0000428852"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         241
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  29043 MW;  A6817F3BFBDF50E5 CRC64;
     MTAASTTATT VLQATQSDVL QEIQSNFLLN SSIWVNIALA GVVILLFVAM GRDLESPRAK
     LIWVATMLVP LVSISSYAGL ASGLTVGFLQ MPPGHALAGQ EVLSPWGRYL TWTFSTPMIL
     LALGLLADTD IASLFTAITM DIGMCVTGLA AALITSSHLL RWVFYGISCA FFVAVLYVLL
     VQWPADAEAA GTSEIFGTLK ILTVVLWLGY PILWALGSEG VALLSVGVTS WGYSGLDILA
     KYVFAFLLLR WVAANEGTVS GSGMGIGSGG ATPADD
 
 
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