4FME

EspG-Rab1-Arf6 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004197	molecular_function	cysteine-type endopeptidase activity
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
C	0000166	molecular_function	nucleotide binding
C	0001726	cellular_component	ruffle
C	0003924	molecular_function	GTPase activity
C	0003925	molecular_function	G protein activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005768	cellular_component	endosome
C	0005769	cellular_component	early endosome
C	0005794	cellular_component	Golgi apparatus
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005925	cellular_component	focal adhesion
C	0005938	cellular_component	cell cortex
C	0006886	biological_process	intracellular protein transport
C	0007155	biological_process	cell adhesion
C	0007399	biological_process	nervous system development
C	0010008	cellular_component	endosome membrane
C	0010975	biological_process	regulation of neuron projection development
C	0010976	biological_process	positive regulation of neuron projection development
C	0015031	biological_process	protein transport
C	0016020	cellular_component	membrane
C	0016192	biological_process	vesicle-mediated transport
C	0016787	molecular_function	hydrolase activity
C	0019003	molecular_function	GDP binding
C	0030139	cellular_component	endocytic vesicle
C	0030154	biological_process	cell differentiation
C	0030496	cellular_component	midbody
C	0030838	biological_process	positive regulation of actin filament polymerization
C	0030866	biological_process	cortical actin cytoskeleton organization
C	0031527	cellular_component	filopodium membrane
C	0031901	cellular_component	early endosome membrane
C	0031996	molecular_function	thioesterase binding
C	0032154	cellular_component	cleavage furrow
C	0032456	biological_process	endocytic recycling
C	0034394	biological_process	protein localization to cell surface
C	0035020	biological_process	regulation of Rac protein signal transduction
C	0035591	molecular_function	signaling adaptor activity
C	0036010	biological_process	protein localization to endosome
C	0048261	biological_process	negative regulation of receptor-mediated endocytosis
C	0048488	biological_process	synaptic vesicle endocytosis
C	0050714	biological_process	positive regulation of protein secretion
C	0051301	biological_process	cell division
C	0051489	biological_process	regulation of filopodium assembly
C	0051549	biological_process	positive regulation of keratinocyte migration
C	0055037	cellular_component	recycling endosome
C	0055038	cellular_component	recycling endosome membrane
C	0060998	biological_process	regulation of dendritic spine development
C	0070062	cellular_component	extracellular exosome
C	0072659	biological_process	protein localization to plasma membrane
C	0090543	cellular_component	Flemming body
C	0097178	biological_process	ruffle assembly
C	0098793	cellular_component	presynapse
C	0098794	cellular_component	postsynapse
C	0098978	cellular_component	glutamatergic synapse
C	0099562	biological_process	maintenance of postsynaptic density structure
C	0120183	biological_process	positive regulation of focal adhesion disassembly
C	1903078	biological_process	positive regulation of protein localization to plasma membrane
C	1903438	biological_process	positive regulation of mitotic cytokinetic process
C	1905345	biological_process	protein localization to cleavage furrow
C	1905606	biological_process	regulation of presynapse assembly
C	1990090	biological_process	cellular response to nerve growth factor stimulus
C	2000009	biological_process	negative regulation of protein localization to cell surface
C	2000171	biological_process	negative regulation of dendrite development
D	0004197	molecular_function	cysteine-type endopeptidase activity
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
F	0000166	molecular_function	nucleotide binding
F	0001726	cellular_component	ruffle
F	0003924	molecular_function	GTPase activity
F	0003925	molecular_function	G protein activity
F	0005515	molecular_function	protein binding
F	0005525	molecular_function	GTP binding
F	0005737	cellular_component	cytoplasm
F	0005768	cellular_component	endosome
F	0005769	cellular_component	early endosome
F	0005794	cellular_component	Golgi apparatus
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0005925	cellular_component	focal adhesion
F	0005938	cellular_component	cell cortex
F	0006886	biological_process	intracellular protein transport
F	0007155	biological_process	cell adhesion
F	0007399	biological_process	nervous system development
F	0010008	cellular_component	endosome membrane
F	0010975	biological_process	regulation of neuron projection development
F	0010976	biological_process	positive regulation of neuron projection development
F	0015031	biological_process	protein transport
F	0016020	cellular_component	membrane
F	0016192	biological_process	vesicle-mediated transport
F	0016787	molecular_function	hydrolase activity
F	0019003	molecular_function	GDP binding
F	0030139	cellular_component	endocytic vesicle
F	0030154	biological_process	cell differentiation
F	0030496	cellular_component	midbody
F	0030838	biological_process	positive regulation of actin filament polymerization
F	0030866	biological_process	cortical actin cytoskeleton organization
F	0031527	cellular_component	filopodium membrane
F	0031901	cellular_component	early endosome membrane
F	0031996	molecular_function	thioesterase binding
F	0032154	cellular_component	cleavage furrow
F	0032456	biological_process	endocytic recycling
F	0034394	biological_process	protein localization to cell surface
F	0035020	biological_process	regulation of Rac protein signal transduction
F	0035591	molecular_function	signaling adaptor activity
F	0036010	biological_process	protein localization to endosome
F	0048261	biological_process	negative regulation of receptor-mediated endocytosis
F	0048488	biological_process	synaptic vesicle endocytosis
F	0050714	biological_process	positive regulation of protein secretion
F	0051301	biological_process	cell division
F	0051489	biological_process	regulation of filopodium assembly
F	0051549	biological_process	positive regulation of keratinocyte migration
F	0055037	cellular_component	recycling endosome
F	0055038	cellular_component	recycling endosome membrane
F	0060998	biological_process	regulation of dendritic spine development
F	0070062	cellular_component	extracellular exosome
F	0072659	biological_process	protein localization to plasma membrane
F	0090543	cellular_component	Flemming body
F	0097178	biological_process	ruffle assembly
F	0098793	cellular_component	presynapse
F	0098794	cellular_component	postsynapse
F	0098978	cellular_component	glutamatergic synapse
F	0099562	biological_process	maintenance of postsynaptic density structure
F	0120183	biological_process	positive regulation of focal adhesion disassembly
F	1903078	biological_process	positive regulation of protein localization to plasma membrane
F	1903438	biological_process	positive regulation of mitotic cytokinetic process
F	1905345	biological_process	protein localization to cleavage furrow
F	1905606	biological_process	regulation of presynapse assembly
F	1990090	biological_process	cellular response to nerve growth factor stimulus
F	2000009	biological_process	negative regulation of protein localization to cell surface
F	2000171	biological_process	negative regulation of dendrite development

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AF3 B 201

Chain	Residue
A	ARG208
A	HOH401
B	SER20
B	GLY21
B	LYS24
B	THR43
B	GDP202
B	MG203
B	HOH301

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP B 202

Chain	Residue
A	ARG208
A	THR239
B	ASP19
B	GLY21
B	VAL22
B	GLY23
B	LYS24
B	SER25
B	CYS26
B	TYR36
B	GLU38
B	ASN124
B	LYS125
B	ASP127
B	LEU128
B	SER154
B	ALA155
B	LYS156
B	AF3201
B	MG203
B	HOH301

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 203

Chain	Residue
B	SER25
B	THR43
B	ASP66
B	AF3201
B	GDP202
B	HOH301

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GTP C 201

Chain	Residue
C	LEU21
C	ASP22
C	ALA23
C	ALA24
C	GLY25
C	LYS26
C	THR27
C	THR28
C	THR41
C	PRO43
C	THR44
C	GLY65
C	GLY66
C	ASN122
C	LYS123
C	ASP125
C	LEU126
C	CYS155
C	ALA156
C	THR157
C	MG202

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 202

Chain	Residue
C	THR27
C	THR44
C	GTP201

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE AF3 E 201

Chain	Residue
D	ARG208
D	HOH401
E	SER20
E	GLY21
E	LYS24
E	THR43
E	GDP202
E	MG203
E	HOH301

---

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP E 202

Chain	Residue
D	ARG208
D	THR239
E	ASP19
E	GLY21
E	VAL22
E	GLY23
E	LYS24
E	SER25
E	CYS26
E	TYR36
E	GLU38
E	ASN124
E	LYS125
E	ASP127
E	LEU128
E	SER154
E	ALA155
E	LYS156
E	AF3201
E	MG203
E	HOH301

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 203

Chain	Residue
E	SER25
E	THR43
E	ASP66
E	AF3201
E	GDP202
E	HOH301

---

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GTP F 201

Chain	Residue
F	ALA24
F	GLY25
F	LYS26
F	THR27
F	THR28
F	THR41
F	PRO43
F	THR44
F	GLY65
F	GLY66
F	ASN122
F	LYS123
F	ASP125
F	LEU126
F	CYS155
F	ALA156
F	THR157
F	MG202
F	LEU21
F	ASP22
F	ALA23

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 202

Chain	Residue
F	THR27
F	THR44
F	GTP201

---

Functional Information from PROSITE/UniProt

site_id	PS00675
Number of Residues	14
Details	SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. LLLiGDSGVGKscL

Chain	Residue	Details
B	LEU14-LEU27

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	28
Details	Motif: {"description":"Switch 1","evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	34
Details	Motif: {"description":"Switch 2","evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SFV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23821544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2FOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23821544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22416225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23588383","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human RAB1A in complex with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3TKL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FMD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FME","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JVS","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"(Microbial infection) O-(2-cholinephosphoryl)serine","evidences":[{"source":"PubMed","id":"21822290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22158903","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"32504010","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	Glycosylation: {"description":"(Microbial infection) N-beta-linked (GlcNAc) arginine","evidences":[{"source":"PubMed","id":"32504010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32974215","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P51153","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16099990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19644450","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21170023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22939626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23940353","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---