8JIA

Cryo-EM structure of Mycobacterium tuberculosis ATP bound FtsE(E165Q)X/RipC complex in peptidisc

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005886	cellular_component	plasma membrane
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0022857	molecular_function	transmembrane transporter activity
A	0030145	molecular_function	manganese ion binding
A	0051301	biological_process	cell division
A	0055085	biological_process	transmembrane transport
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005886	cellular_component	plasma membrane
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0022857	molecular_function	transmembrane transporter activity
B	0030145	molecular_function	manganese ion binding
B	0051301	biological_process	cell division
B	0055085	biological_process	transmembrane transport
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016020	cellular_component	membrane
C	0051301	biological_process	cell division
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016020	cellular_component	membrane
D	0051301	biological_process	cell division
E	0005576	cellular_component	extracellular region
E	0006508	biological_process	proteolysis
E	0008233	molecular_function	peptidase activity
E	0008234	molecular_function	cysteine-type peptidase activity
E	0008745	molecular_function	N-acetylmuramoyl-L-alanine amidase activity
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0016787	molecular_function	hydrolase activity
E	0071554	biological_process	cell wall organization or biogenesis

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU140-PHE154

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01284","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	92
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	160
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	308
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---