hlyB

Functionⁱ

Part of the ABC transporter complex HlyBD involved in hemolysin export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (By similarity).By similarity

Miscellaneous

The complex HlyBD-TolC (OMF) forms a single transport channel across the two membranes, allowing direct export of alpha-hemolysin. These channel is involved in type 1 secretion system (By similarity).By similarity

Caution

Tyr-9 is present instead of the conserved Cys which is expected to be the active site residue of peptidase C39. Thus they are presumed to be without peptidase activity.Curated

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	83	PROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	502 – 509	ATPPROSITE-ProRule annotation		8

GO - Molecular functionⁱ

ATPase activity, coupled to transmembrane movement of substances Source: InterPro
ATP binding Source: UniProtKB-KW
peptidase activity Source: InterPro
protein transporter activity Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

protein secretion by the type I secretion system Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Transport
Ligand	ATP-binding, Nucleotide-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Alpha-hemolysin translocation ATP-binding protein HlyB
Gene namesⁱ	Name:hlyB
Organismⁱ	Escherichia coli
Taxonomic identifierⁱ	562 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia

Subcellular locationⁱ

Cell inner membrane Curated; Multi-pass membrane protein Curated

Topology

Feature key	Position(s)	DescriptionActions	Length
Transmembraneⁱ	158 – 178	HelicalPROSITE-ProRule annotationAdd BLAST	21
Transmembraneⁱ	191 – 211	HelicalPROSITE-ProRule annotationAdd BLAST	21
Transmembraneⁱ	269 – 289	HelicalPROSITE-ProRule annotationAdd BLAST	21
Transmembraneⁱ	295 – 315	HelicalPROSITE-ProRule annotationAdd BLAST	21
Transmembraneⁱ	388 – 408	HelicalPROSITE-ProRule annotationAdd BLAST	21

GO - Cellular componentⁱ

integral component of membrane Source: UniProtKB-KW
plasma membrane Source: UniProtKB-SubCell
type I protein secretion system complex Source: InterPro

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000092373	1 – 707	Alpha-hemolysin translocation ATP-binding protein HlyBAdd BLAST		707

Interactionⁱ

Subunit structureⁱ

Homodimer.By similarity

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	9 – 20	Combined sources	12
Helixⁱ	27 – 33	Combined sources	7
Helixⁱ	43 – 51	Combined sources	9
Turnⁱ	52 – 54	Combined sources	3
Beta strandⁱ	55 – 61	Combined sources	7
Helixⁱ	64 – 67	Combined sources	4
Beta strandⁱ	70 – 76	Combined sources	7
Beta strandⁱ	84 – 89	Combined sources	6
Turnⁱ	91 – 93	Combined sources	3
Beta strandⁱ	94 – 100	Combined sources	7
Turnⁱ	101 – 104	Combined sources	4
Beta strandⁱ	105 – 110	Combined sources	6
Helixⁱ	111 – 117	Combined sources	7
Beta strandⁱ	120 – 129	Combined sources	10

3D structure databases

ProteinModelPortalⁱ	Q47258
SMRⁱ	Q47258
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	3 – 125	Peptidase C39PROSITE-ProRule annotationAdd BLAST	123
Domainⁱ	154 – 436	ABC transmembrane type-1PROSITE-ProRule annotationAdd BLAST	283
Domainⁱ	468 – 703	ABC transporterPROSITE-ProRule annotationAdd BLAST	236

Domainⁱ

In HlyB the peptidase C39 domain, the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.

Sequence similaritiesⁱ

Belongs to the ABC transporter superfamily. Protein-1 exporter (TC 3.A.1.109) family. [View classification]Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4108JJA Bacteria COG2274 LUCA

eggNOGⁱ

ENOG4108JJA Bacteria
COG2274 LUCA

Family and domain databases

Gene3Dⁱ	1.20.1560.10, 1 hit
InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR011527 ABC1_TM_dom IPR036640 ABC1_TM_sf IPR003439 ABC_transporter-like IPR017871 ABC_transporter_CS IPR010132 ATPase_T1SS_HlyB IPR027417 P-loop_NTPase IPR005074 Peptidase_C39
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00664 ABC_membrane, 1 hit PF00005 ABC_tran, 1 hit PF03412 Peptidase_C39, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit SSF90123 SSF90123, 1 hit
TIGRFAMsⁱ	TIGR01846 type_I_sec_HlyB, 1 hit
PROSITEⁱ	View protein in PROSITE PS50929 ABC_TM1F, 1 hit PS00211 ABC_TRANSPORTER_1, 1 hit PS50893 ABC_TRANSPORTER_2, 1 hit PS50990 PEPTIDASE_C39, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q47258-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MDSCHKIDYG LYALEILAQY HNVSVNPEEI KHRFDTDGTG LGLTSWLLAA 
        60         70         80         90        100
KSLELKVKQV KKTIDRLNFI SLPALVWRED GRHFILTKVS KEANRYLIFD 
       110        120        130        140        150
LEQRNPRVLE QSEFEALYQG HIILIASRSS VAGKLAKFDF TWFIPAIIKY 
       160        170        180        190        200
RRIFIETLVV SVFLQLFALI TPLFFQVVMD KVLVHRGFST LNVITVALSV 
       210        220        230        240        250
VVVFEIILSG LRTYIFAHST SRIDVELGAK LFRHLLALPI SYFESRRVGD 
       260        270        280        290        300
TVARVRELDQ IRNFLTGQAL TSVLDLLFSF IFFAVMWYYS PKLTLVILFS 
       310        320        330        340        350
LPCYAAWSVF ISPILRRRLD DKFSRNADNQ SFLVESVTAI NTIKAMAVSP 
       360        370        380        390        400
QMTNIWDKQL AGYVAAGFKV TVLATIGQQG IQLIQKTVMI INLWLGAHLV 
       410        420        430        440        450
ISGDLSIGQL IAFNMLAGQI VAPVIRLAQI WQDFQQVGIS VTRLGDVLNS 
       460        470        480        490        500
PTESYHGKLA LPEINGDITF RNIRFRYKPD SPVILDNINL SIKQGEVIGI 
       510        520        530        540        550
VGRSGSGKST LTKLIQRFYI PENGQVLIDG HDLALADPNW LRRQVGVVLQ 
       560        570        580        590        600
DNVLLNRSII DNISLANPGM SVEKVIYAAK LAGAHDFISE LREGYNTIVG 
       610        620        630        640        650
EQGAGLSGGQ RQRIAIARAL VNNPKILIFD EATSALDYES EHIIMRNMHK 
       660        670        680        690        700
ICKGRTVIII AHRLSTVKNA DRIIVMEKGK IVEQGKHKEL LSEPESLYSY 

LYQLQSD

Length:707

Mass (Da):79,529

Last modified:November 1, 1996 - v1

Checksum:ⁱE709E59F21BDA853

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M81823 Genomic DNA Translation: AAA23978.1
PIRⁱ	A42255 LEECB
NCBI Reference Sequences More...RefSeqⁱ	WP_000376543.1, NZ_PXWC01000014.1

Protein	Similar proteins		Species	Score	Length
Q47258	Peptidase C39		ECOLX		707
Hemolysin secretion protein HlyB		ECOUT		707
UPI000A3A2F75		ECOLX		430
UPI0005A84E55		ECOLX		124
UPI000B3DFE71		ECOLX		568
+4

Protein	Similar proteins		Species	Score	Length
Q47258	Alpha-hemolysin translocation ATP-binding protein HlyB	)	ECOLX		707
Alpha-hemolysin translocation ATP-binding protein HlyB		SHIBO		707
Alpha-hemolysin translocation ATP-binding protein HlyB		Escherichia coli 2.3916		719
Hemolysin secretion protein HlyB		ECOUT		707
Alpha-hemolysin translocation ATP-binding protein HlyB		ECOL6		707
+125

Protein	Similar proteins		Species	Score	Length
Q47258	Toxin RTX-III translocation ATP-binding protein		ACTPL		711
Type I secretion system permease/ATPase		Actinobacillus seminis		711
Exotoxin translocation ATP-binding protein PaxB		PASAE		711
Alpha-hemolysin translocation ATP-binding protein hlyB		Actinobacillus pleuropneumoniae serovar 4 str. M62		711
Toxin RTX-III translocation ATP-binding protein (RTX-III toxin determinant B)		ACTPJ		707
+440

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M81823 Genomic DNA Translation: AAA23978.1
PIRⁱ	A42255 LEECB
NCBI Reference Sequences More...RefSeqⁱ	WP_000376543.1, NZ_PXWC01000014.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3ZUA	NMR	-	A	2-137	[»]
ProteinModelPortalⁱ	Q47258
SMRⁱ	Q47258
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Phylogenomic databases

eggNOGⁱ	ENOG4108JJA Bacteria COG2274 LUCA

eggNOGⁱ

ENOG4108JJA Bacteria
COG2274 LUCA

Family and domain databases

Gene3Dⁱ	1.20.1560.10, 1 hit
InterProⁱ	View protein in InterPro IPR003593 AAA+_ATPase IPR011527 ABC1_TM_dom IPR036640 ABC1_TM_sf IPR003439 ABC_transporter-like IPR017871 ABC_transporter_CS IPR010132 ATPase_T1SS_HlyB IPR027417 P-loop_NTPase IPR005074 Peptidase_C39
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00664 ABC_membrane, 1 hit PF00005 ABC_tran, 1 hit PF03412 Peptidase_C39, 1 hit
SMARTⁱ	View protein in SMART SM00382 AAA, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit SSF90123 SSF90123, 1 hit
TIGRFAMsⁱ	TIGR01846 type_I_sec_HlyB, 1 hit
PROSITEⁱ	View protein in PROSITE PS50929 ABC_TM1F, 1 hit PS00211 ABC_TRANSPORTER_1, 1 hit PS50893 ABC_TRANSPORTER_2, 1 hit PS50990 PEPTIDASE_C39, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HLYB3_ECOLX
Accessionⁱ	Q47258Primary (citable) accession number: Q47258
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
	Last sequence update:	November 1, 1996
	Last modified:	July 18, 2018
	This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - Q47258 (HLYB3_ECOLX)

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Alpha-hemolysin translocation ATP-binding protein HlyB

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Caution

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ