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3.E.1.2.2
Chloride-pumping halorhodopsin (a trimer with the carotenoid, bacterioruberin, binding to crevices between adjacent protein subunits in the trimeric assembly; Sasaki et al., 2012). Structure known to 2.0 Å resolution (Kouyama et al., 2010) (PDB# 3A7K)). In addition to Cl-, it pumps Br-, I- and NO3- (Kikukawa 2021).  Helix movement is required to create the Cl- entrance path on the extracellular surface of the protein and is crucial for the Cl- uptake process (Zhang et al. 2024).

Accession Number:P15647
Protein Name:Halorhodopsin
Length:291
Molecular Weight:31080.00
Species:Natronomonas pharaonis (Natronobacterium pharaonis) [2257]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate chloride, bromide, iodide, nitric acid

Cross database links:

Pfam: PF01036   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005216 F:ion channel activity
GO:0009881 F:photoreceptor activity
GO:0006811 P:ion transport
GO:0007602 P:phototransduction
GO:0018298 P:protein-chromophore linkage

References (2)

[1] “The primary structure of a halorhodopsin from Natronobacterium pharaonis. Structural, functional and evolutionary implications for bacterial rhodopsins and halorhodopsins.”  Lanyi J.K.et.al.   2104837
[2] “Blue halorhodopsin from Natronobacterium pharaonis: wavelength regulation by anions.”  Scharf B.et.al.   8204571
Structure:
3QBG   3QBI   3QBK   3QBL   3VVK   3a7k     

External Searches:

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MTETLPPVTE SAVALQAEVT QRELFEFVLN DPLLASSLYI NIALAGLSIL LFVFMTRGLD 
61:	DPRAKLIAVS TILVPVVSIA SYTGLASGLT ISVLEMPAGH FAEGSSVMLG GEEVDGVVTM 
121:	WGRYLTWALS TPMILLALGL LAGSNATKLF TAITFDIAMC VTGLAAALTT SSHLMRWFWY 
181:	AISCACFLVV LYILLVEWAQ DAKAAGTADM FNTLKLLTVV MWLGYPIVWA LGVEGIAVLP 
241:	VGVTSWGYSF LDIVAKYIFA FLLLNYLTSN ESVVSGSILD VPSASGTPAD D