2LZR

TatA T22P

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	MttA_Hcf106	e2lzrA1	A: extended segments	X: Twin-arginine transport (Tat) system component TatA (From Topology)	H: Twin-arginine transport (Tat) system component TatA (From Topology)	T: Twin-arginine transport (Tat) system component TatA	F: MttA_Hcf106	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.5.3310	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02416	mttA/Hcf106 family (TatA_B_E)	mttA/Hcf106 family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Sec-independent protein translocase protein TatA	binding lipid binding macromolecule transmembrane transporter activity protein transporter activity protein transmembrane transporter activity transporter activity transmembrane transporter activity active transmembrane transporter activity proton motive force dependent protein transmembrane transporter activity secondary active transmembrane transporter activity identical protein binding protein binding	protein localization establishment of protein localization cellular localization nitrogen compound transport transport establishment of localization transmembrane transport localization protein transmembrane transport protein transport protein transport by the Tat complex cellular macromolecule localization macromolecule localization cellular process protein localization establishment of protein localization cellular localization nitrogen compound transport transport establishment of localization transmembrane transport localization protein transmembrane transport protein transport protein transport by the Tat complex cellular macromolecule localization macromolecule localization cellular process intracellular protein transmembrane transport intracellular transport establishment of localization in cell intracellular protein transport	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane protein-containing complex plasma membrane protein complex membrane protein complex TAT protein transport complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR006312	Sec-independent protein translocase protein TatA/E	Family
A	IPR003369	Sec-independent protein translocase protein TatA/B/E	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Transmembrane	Alpha-helical polytopic	Twin arginine targeting (Tat) family	TatA/TatB family

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	Sec, Translocase, and Insertase Proteins	TatA twin-arginine translocase, model of oligomeric complex

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A	FME	Parent Component: MET RESID: AA0021 , AA0566 PSI-MOD : N-formyl-L-methionine residue MOD:00030 , N-formyl-L-methionine (Met) MOD:00482 , N-[(L-histidin-1'-yl)methyl]-L-methionine (fMet) MOD:01890 , N-[(L-histidin-1'-yl)methyl]-L-methionine (Met) MOD:01891

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.