4QL0

Crystal Structure Analysis of the Membrane Transporter FhaC (double mutant V169T, I176N)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
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

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Outer-membrane protein Omp85-like	8045036	4006144	SCOP2 (2022-06-29)
A	SCOP2 Family	POTRA domain-like	8046795	4006413	SCOP2 (2022-06-29)
A	SCOP2 Family	POTRA domain-like	8050917	4006413	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Porins	8052279	3000224	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	POTRA domain-like	8052280	3002100	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	POTRA domain-like	8052281	3002100	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	ShlB	e4ql0A3	A: beta barrels	X: Outer membrane meander beta-barrels	H: Porins	T: Porin	F: ShlB	ECOD (1.6)
A	POTRA_2	e4ql0A1	A: a+b duplicates or obligate multimers	X: Polypeptide transport-associated (POTRA) domain (From Topology)	H: Polypeptide transport-associated (POTRA) domain (From Topology)	T: Polypeptide transport-associated (POTRA) domain	F: POTRA_2	ECOD (1.6)
A	POTRA_3	e4ql0A2	A: a+b duplicates or obligate multimers	X: Polypeptide transport-associated (POTRA) domain (From Topology)	H: Polypeptide transport-associated (POTRA) domain (From Topology)	T: Polypeptide transport-associated (POTRA) domain	F: POTRA_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.20.310	Alpha Beta	Roll	Ubiquitin-like (UB roll)	membrane protein fhac	CATH (utative)
A	2.40.160.50	Mainly Beta	Beta Barrel	Porin	membrane protein fhac: a member of the omp85/tpsb transporter family	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF17287	POTRA domain (POTRA_3)	POTRA domain	This POTRA domain is found in ShlB-like proteins.	Domain
A	PF03865	Haemolysin secretion/activation protein ShlB/FhaC/HecB (ShlB)	Haemolysin secretion/activation protein ShlB/FhaC/HecB	-	Family
A	PF08479	POTRA domain, ShlB-type (POTRA_2)	POTRA domain, ShlB-type	The POTRA domain (for polypeptide-transport-associated domain) is found towards the N-terminus of ShlB family proteins (Pfam:PF03865). ShlB is important in the secretion and activation of the haemolysin ShlA. It has been postulated that the POTRA dom ...	The POTRA domain (for polypeptide-transport-associated domain) is found towards the N-terminus of ShlB family proteins (Pfam:PF03865). ShlB is important in the secretion and activation of the haemolysin ShlA. It has been postulated that the POTRA domain has a chaperone-like function over ShlA; it may fold back into the C-terminal beta-barrel channel [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Filamentous hemagglutinin transporter protein FhaC	wide pore channel activity passive transmembrane transporter activity channel activity porin activity transporter activity transmembrane transporter activity macromolecule transmembrane transporter activity protein transporter activity protein transmembrane transporter activity	localization transport monoatomic ion transport establishment of localization protein localization protein transport across the cell outer membrane establishment of protein localization cellular localization nitrogen compound transport secretion establishment of protein localization to extracellular region export from cell protein secretion protein localization to extracellular region localization transport monoatomic ion transport establishment of localization protein localization protein transport across the cell outer membrane establishment of protein localization cellular localization nitrogen compound transport secretion establishment of protein localization to extracellular region export from cell protein secretion protein localization to extracellular region protein secretion by the type V secretion system transmembrane transport secretion by cell protein transmembrane transport protein transport cellular macromolecule localization macromolecule localization cellular process	type V protein secretion system complex protein-containing complex cellular anatomical structure membrane pore complex membrane protein complex cell periphery cell outer membrane external encapsulating structure cell envelope outer membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR034746	POTRA domain	Domain
A	IPR005565	Haemolysin activator HlyB, C-terminal	Domain
A	IPR051544	Two-partner secretion system outer membrane transporter	Family
A	IPR027282	Two partner secretion pathway transporter	Family
A	IPR013686	Polypeptide-transport-associated, ShlB-type	Domain
A	IPR035251	ShlB, POTRA domain	Domain

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Transmembrane	Beta-barrel transmembrane	Omp85-TpsB transporters (n=16,S=20,22)	Two-partner secretion porin (n=16,S=20)

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

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.