Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyHP1076-like8045704 4004628 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyFlgL-like8091605 3002287 SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF16522e3k1hA1 A: alpha bundlesX: Four-helical up-and-down bundleH: alpha-helical domain in phase 1 flagellin (From Topology)T: alpha-helical domain in phase 1 flagellinF: PF16522ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.30.1120.180 Alpha Beta 2-Layer Sandwich Arylsulfatase, C-terminal domain Flagellar FLiS export co-chaperone, HP1076CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF16522Flagellar FLiS export co-chaperone, HP1076 (FliS_cochap)Flagellar FLiS export co-chaperone, HP1076FliS_cochap is a family of largely Campylobacterales proteins that are co-chaperones for FliS, one of the type III secretion system flagellar chaperones. The HP1076 (Flis_cochap) and FliS complex together prevents premature polymerisation of flagelli ...FliS_cochap is a family of largely Campylobacterales proteins that are co-chaperones for FliS, one of the type III secretion system flagellar chaperones. The HP1076 (Flis_cochap) and FliS complex together prevents premature polymerisation of flagellins and is critical for flagellar assembly and bacterial colonisation. The HP1076 shows co-chaperone activity that promotes protein folding of FliS with mutations in the flagellin binding pocket and enhances the chaperone activity of FliS [1].
Domain

InterPro: Protein Family Classification InterPro Database Homepage