4UAQ

Crystal structure of the accessory translocation ATPase, SecA2, from Mycobacterium tuberculosis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006605	biological_process	protein targeting
A	0006886	biological_process	intracellular protein transport
A	0008320	molecular_function	protein transmembrane transporter activity
A	0008564	molecular_function	protein-exporting ATPase activity
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0017038	biological_process	protein import
A	0031522	cellular_component	cell envelope Sec protein transport complex
A	0043952	biological_process	protein transport by the Sec complex
A	0051701	biological_process	biological process involved in interaction with host
A	0052170	biological_process	symbiont-mediated suppression of host innate immune response
A	0052553	biological_process	symbiont-mediated perturbation of host immune response
A	0065002	biological_process	intracellular protein transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS01312
Number of Residues	16
Details	SECA SecA family signature. VtVSTQMAGRGtDIrL

Chain	Residue	Details
A	VAL493-LEU508

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382

Chain	Residue	Details
A	GLN94
A	GLY112
A	ASP505

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