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Sensory rhodopsin III (HmSRIII) (Opsin) (Sensory-like rhodopsin) (HmSMR)

 BACS3_HALMA             Reviewed;         232 AA.
Q5V4H7;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
16-JAN-2019, entry version 56.
RecName: Full=Sensory rhodopsin III;
Short=HmSRIII;
AltName: Full=Opsin;
AltName: Full=Sensory-like rhodopsin;
Short=HmSMR;
Name=xop2; Synonyms=sop3; OrderedLocusNames=rrnAC0559;
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
B-1809) (Halobacterium marismortui).
Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
Halobacteriales; Haloarculaceae; Haloarcula.
NCBI_TaxID=272569;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
PubMed=15520287; DOI=10.1101/gr.2700304;
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G.,
Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P.,
Date S.V., Marcotte E., Hood L., Ng W.V.;
"Genome sequence of Haloarcula marismortui: a halophilic archaeon from
the Dead Sea.";
Genome Res. 14:2221-2234(2004).
[2]
FUNCTION, INDUCTION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES,
AND INTERACTION WITH HTRM.
PubMed=20802037; DOI=10.1128/JB.00642-10;
Fu H.Y., Lin Y.C., Chang Y.N., Tseng H., Huang C.C., Liu K.C.,
Huang C.S., Su C.W., Weng R.R., Lee Y.Y., Ng W.V., Yang C.S.;
"A novel six-rhodopsin system in a single archaeon.";
J. Bacteriol. 192:5866-5873(2010).
[3]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND NOMENCLATURE.
PubMed=20880715; DOI=10.1016/j.jphotobiol.2010.09.004;
Nakao Y., Kikukawa T., Shimono K., Tamogami J., Kimitsuki N., Nara T.,
Unno M., Ihara K., Kamo N.;
"Photochemistry of a putative new class of sensory rhodopsin (SRIII)
coded by xop2 of Haloarcular marismortui.";
J. Photochem. Photobiol. B 102:45-54(2011).
-!- FUNCTION: Sensory rhodopsin. Associates with an unusual transducer
lacking a methyl-accepting transducer domain found in all other
photosensory transducers. The chromophore is all-trans-retinal in
the dark. {ECO:0000269|PubMed:20802037,
ECO:0000269|PubMed:20880715}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=506 nm {ECO:0000269|PubMed:20802037,
ECO:0000269|PubMed:20880715};
-!- SUBUNIT: Interacts with HtrM. {ECO:0000269|PubMed:20802037}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- INDUCTION: Expressed constitutively throughout the growth phases,
both in presence and absence of white light.
{ECO:0000269|PubMed:20802037}.
-!- PTM: The covalent binding of retinal to the apoprotein,
bacterioopsin, generates bacteriorhodopsin. {ECO:0000250}.
-!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
{ECO:0000305}.
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EMBL; AY596297; AAV45575.1; -; Genomic_DNA.
RefSeq; WP_004962072.1; NC_006396.1.
ProteinModelPortal; Q5V4H7; -.
STRING; 272569.rrnAC0559; -.
TCDB; 3.E.1.3.4; the ion-translocating microbial rhodopsin (mr) family.
EnsemblBacteria; AAV45575; AAV45575; rrnAC0559.
GeneID; 3130491; -.
KEGG; hma:rrnAC0559; -.
PATRIC; fig|272569.17.peg.1323; -.
eggNOG; arCOG02810; Archaea.
eggNOG; COG5524; LUCA.
KO; K04643; -.
Proteomes; UP000001169; Chromosome I.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005216; F:ion channel activity; IEA:InterPro.
GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
InterPro; IPR001425; Arc/bac/fun_rhodopsins.
PANTHER; PTHR28286; PTHR28286; 1.
Pfam; PF01036; Bac_rhodopsin; 1.
PRINTS; PR00251; BACTRLOPSIN.
SMART; SM01021; Bac_rhodopsin; 1.
1: Evidence at protein level;
Chromophore; Complete proteome; Membrane; Photoreceptor protein;
Receptor; Reference proteome; Retinal protein; Sensory transduction;
Transmembrane; Transmembrane helix.
CHAIN 1 232 Sensory rhodopsin III.
/FTId=PRO_0000428855.
TRANSMEM 5 25 Helical. {ECO:0000255}.
TRANSMEM 39 59 Helical. {ECO:0000255}.
TRANSMEM 73 93 Helical. {ECO:0000255}.
TRANSMEM 100 120 Helical. {ECO:0000255}.
TRANSMEM 125 145 Helical. {ECO:0000255}.
TRANSMEM 168 188 Helical. {ECO:0000255}.
TRANSMEM 194 214 Helical. {ECO:0000255}.
SITE 75 75 Primary proton acceptor. {ECO:0000250}.
MOD_RES 205 205 N6-(retinylidene)lysine. {ECO:0000250}.
SEQUENCE 232 AA; 25084 MW; 198AD3B352481652 CRC64;
MAQEIVWYGA GAGAFFVSAV VFVWFAATRG NIRSSFYYLP PIHTSVAGAA YVAMALIAGG
QLGDTVSITT LRFADWIVST PIITYYLARL AGVDTQTRRL AVAANVVMIG VGYGFVSMSG
SLRWIAFAVS TVAFIGLLYL YIKTFARKIN AATASVRSLF QSLRDLTVVT WSLYPVVYFL
GPLGTGIIQA PDLNFLVAVL DTIAKVGFMS ILLVRYNSVE TFVDSWSVAP AK


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