7M33

The structure of Bacillus subtilis BmrCD in the inward-facing conformation bound to Hoechst-33342 and ATP

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0005524	molecular_function	ATP binding
C	0005886	cellular_component	plasma membrane
C	0016020	cellular_component	membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
C	0046677	biological_process	response to antibiotic
C	0055085	biological_process	transmembrane transport
C	0140359	molecular_function	ABC-type transporter activity
D	0005524	molecular_function	ATP binding
D	0005886	cellular_component	plasma membrane
D	0006869	biological_process	lipid transport
D	0016020	cellular_component	membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
D	0046677	biological_process	response to antibiotic
D	0055085	biological_process	transmembrane transport
D	0140359	molecular_function	ABC-type transporter activity

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRISIARAL

Chain	Residue	Details
C	LEU475-LEU489
D	LEU567-LEU581

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	100
Details	TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441

Chain	Residue	Details
D	LEU18-ILE38
D	ILE146-PHE166
D	LEU223-THR243
D	LEU245-LEU265
D	LEU347-VAL367
C	VAL279-ILE299

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434

Chain	Residue	Details
D	GLY463

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