6ITC

Structure of a substrate engaged SecA-SecY protein translocation machine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006605	biological_process	protein targeting
A	0006886	biological_process	intracellular protein transport
A	0008564	molecular_function	protein-exporting ATPase activity
A	0015031	biological_process	protein transport
A	0016020	cellular_component	membrane
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	0045121	cellular_component	membrane raft
A	0046872	molecular_function	metal ion binding
A	0065002	biological_process	intracellular protein transmembrane transport
E	0005886	cellular_component	plasma membrane
E	0006605	biological_process	protein targeting
E	0006886	biological_process	intracellular protein transport
E	0008320	molecular_function	protein transmembrane transporter activity
E	0009306	biological_process	protein secretion
E	0015031	biological_process	protein transport
E	0016020	cellular_component	membrane
E	0043952	biological_process	protein transport by the Sec complex
E	0065002	biological_process	intracellular protein transmembrane transport
G	0006091	biological_process	generation of precursor metabolites and energy
G	0008218	biological_process	bioluminescence
Y	0005886	cellular_component	plasma membrane
Y	0006605	biological_process	protein targeting
Y	0015031	biological_process	protein transport
Y	0016020	cellular_component	membrane
Y	0043952	biological_process	protein transport by the Sec complex
Y	0065002	biological_process	intracellular protein transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue MG A 1001

Chain	Residue
A	BEF1002
A	ADP1003

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site_id	AC2
Number of Residues	9
Details	binding site for residue BEF A 1002

Chain	Residue
A	MG1001
A	ADP1003
A	THR102
A	GLY103
A	ARG489
A	GLY490
A	GLN521
A	ARG525
A	ARG528

---

site_id	AC3
Number of Residues	12
Details	binding site for residue ADP A 1003

Chain	Residue
A	MET79
A	PHE80
A	PHE82
A	GLN85
A	GLY103
A	GLY105
A	LYS106
A	THR107
A	ASP492
A	ARG528
A	MG1001
A	BEF1002

---

site_id	AC4
Number of Residues	1
Details	binding site for residue PGV Y 501

Chain	Residue
Y	ARG362

---

site_id	AC5
Number of Residues	9
Details	binding site for residue PGV Y 502

Chain	Residue
Y	CYS60
Y	ILE187
Y	ILE191
Y	ILE194
Y	ALA221
Y	GLN396
Y	ILE397
Y	SER401
Y	LEU402

---

Functional Information from PROSITE/UniProt

site_id	PS00755
Number of Residues	20
Details	SECY_1 Protein secY signature 1. SIFaMGVmPYItASIIVQLL

Chain	Residue	Details
Y	SER68-LEU87

---

site_id	PS00756
Number of Residues	18
Details	SECY_2 Protein secY signature 2. WLgEqITak.GVGNGiSII

Chain	Residue	Details
Y	TRP165-ILE182

---

site_id	PS01067
Number of Residues	29
Details	SECE_SEC61G Protein secE/sec61-gamma signature. FfKEvVreLkKvsWPnrkElvnytAVVLA

Chain	Residue	Details
E	PHE7-ALA35

---

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

Chain	Residue	Details
A	VAL480-LEU495

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	TOPO_DOM: Periplasmic => ECO:0000269|PubMed:11276254, ECO:0000269|PubMed:9808047

Chain	Residue	Details
B	ALA23-ASP27

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	CROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132

Chain	Residue	Details
G	GYS66
G	GLN69

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01382, ECO:0000269|PubMed:12242434, ECO:0000269|PubMed:15256599, ECO:0000269|PubMed:16989859, ECO:0007744|PDB:1M74, ECO:0007744|PDB:1TF2, ECO:0007744|PDB:2IBM

Chain	Residue	Details
A	ASP492

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