4PL0

Crystal structure of the antibacterial peptide ABC transporter McjD in an outward occluded state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0006869	biological_process	lipid transport
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0030153	biological_process	bacteriocin immunity
A	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
A	0043213	biological_process	bacteriocin transport
A	0055085	biological_process	transmembrane transport
A	0140359	molecular_function	ABC-type transporter activity
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0006869	biological_process	lipid transport
B	0015031	biological_process	protein transport
B	0016020	cellular_component	membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0030153	biological_process	bacteriocin immunity
B	0034040	molecular_function	ATPase-coupled lipid transmembrane transporter activity
B	0043213	biological_process	bacteriocin transport
B	0055085	biological_process	transmembrane transport
B	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. YSGGQKQRISLARLF

Chain	Residue	Details
A	TYR481-PHE495

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU00441

Chain	Residue	Details
A	PHE25-ILE45
A	VAL66-PHE86
A	VAL143-SER163
A	TRP167-LEU187
A	ALA261-VAL281
A	PHE286-LEU306
B	PHE25-ILE45
B	VAL66-PHE86
B	VAL143-SER163
B	TRP167-LEU187
B	ALA261-VAL281
B	PHE286-LEU306

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434

Chain	Residue	Details
A	GLY378
B	GLY378

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