type I protein secretion system complex / protein secretion by the type I secretion system / ATPase-coupled transmembrane transporter activity / peptidase activity / membrane => GO:0016020 / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function
ATPase, type I secretion system, HlyB / Peptidase C39-like A / Peptidase C39 family / Peptidase C39, bacteriocin processing / Peptidase family C39 domain profile. / Cysteine proteinases / Type 1 protein exporter / Cathepsin B; Chain A / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain ...ATPase, type I secretion system, HlyB / Peptidase C39-like A / Peptidase C39 family / Peptidase C39, bacteriocin processing / Peptidase family C39 domain profile. / Cysteine proteinases / Type 1 protein exporter / Cathepsin B; Chain A / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Alpha-Beta Complex / P-loop containing nucleoside triphosphate hydrolase / Alpha Beta Similarity search - Domain/homology
Mass: 16106.483 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: Q47258, papain
Sequence details
AS A RESULT OF CLONING STRATEGY AND PROTEASE DIGESTION, THE SEQUENCE N-TERMINAL TO THE WT POSITION ...AS A RESULT OF CLONING STRATEGY AND PROTEASE DIGESTION, THE SEQUENCE N-TERMINAL TO THE WT POSITION 2 IS GAMANS.
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
NOESY (ALIPHATIC
1
2
1
AROMATIC
1
3
1
AMID)
NMR details
Text: THE STRUCTURE WAS DETERMINED BY NOE DERIVED DISTANCE RESTRAINTS FROM (1H-1H-13C)-NOESY-HSQC ALIPHATIC & AROMATIC AND (1H-15N-1H)-HSQC-NOESY USING CHEMICAL SHIFT ASSIGNMENTS DEPOSITED IN BMRB ENTRY 17403.
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