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3.E.1.1.5 Bacteriorhodopsin I (HmBRI) of 250 aas and 7 TMSs. The structure is known to 2.5 Å resolution, revealing the usual BRI fold but with several modifications (Shevchenko et al. 2014). Expression in E. coli membranes does not affect the overall structure.
Accession Number:	Q5UXY6
Protein Name:	Bacteriorhodopsin-I
Length:	250
Molecular Weight:	26946.00
Species:	Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) [272569]
Number of TMSs:	7
Location¹ / Topology² / Orientation³:	Membrane¹ / Multi-pass membrane protein²
Substrate	hydron

Structure:
4PXK

UniProt (Universal Protein Resource)
CDD Search (Conserved Domain Database)

Predict TMSs (Predict number of transmembrane segments)

FASTA formatted sequence

1:	MPAPGSEGIW LWLGTAGMFL GMLYFIARGW GETDGRRQKF YIATILITAI AFVNYLAMAL 
61:	GFGLTFIEFG GEQHPIYWAR YTDWLFTTPL LLYDLGLLAG ADRNTIYSLV SLDVLMIGTG 
121:	VVATLSAGSG VLSAGAERLV WWGISTAFLL VLLYFLFSSL SGRVANLPSD TRSTFKTLRN 
181:	LVTVVWLVYP VWWLVGSEGL GLVGIGIETA GFMVIDLVAK VGFGIILLRS HGVLDGAAET 
241:	TGTGATPADD

3.E.1.1.5
Bacteriorhodopsin I (HmBRI) of 250 aas and 7 TMSs. The structure is known to 2.5 Å resolution, revealing the usual BRI fold but with several modifications (Shevchenko et al. 2014). Expression in E. coli membranes does not affect the overall structure.

Cross database links:

External Searches:

Analyze:

3.E.1.1.5Bacteriorhodopsin I (HmBRI) of 250 aas and 7 TMSs. The structure is known to 2.5 Å resolution, revealing the usual BRI fold but with several modifications (Shevchenko et al. 2014). Expression in E. coli membranes does not affect the overall structure.

Cross database links:

External Searches:

Analyze:

3.E.1.1.5
Bacteriorhodopsin I (HmBRI) of 250 aas and 7 TMSs. The structure is known to 2.5 Å resolution, revealing the usual BRI fold but with several modifications (Shevchenko et al. 2014). Expression in E. coli membranes does not affect the overall structure.