Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

3 structures for O66663

Entry ID Method Resolution Chain Position Source
2XCI X-ray 200 A A/B/C/D 1-353 PDB
2XCU X-ray 242 A A/B/C/D 1-353 PDB
AF-O66663-F1 Predicted AlphaFoldDB

No variants for O66663

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O66663

No associated diseases with O66663

3 regional properties for O66663

Type Name Position InterPro Accession
domain Regulator of K+ conductance, N-terminal 402 - 524 IPR003148
domain K+/H+ exchanger 14 - 283 IPR004771
domain Cation/H+ exchanger 12 - 373 IPR006153

Functions

Description
EC Number 2.4.99.12 Transferring other glycosyl groups
Subcellular Localization
  • Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
Kdo transferase activity Catalysis of the reactions: (KDO)-lipid IVA + CMP-3-deoxy-D-manno-octulosonate = KDO2-lipid IVA + CMP, and lipid IVA + CMP-3-deoxy-D-manno-octulosonate = (KDO)-lipid IVA + CMP.
transferase activity Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

2 GO annotations of biological process

Name Definition
lipid A biosynthetic process The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
lipopolysaccharide core region biosynthetic process The chemical reactions and pathways resulting in the formation of the core region of bacterial lipopolysaccharides, which contains ten saccharide residues.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQFEVLKRFF PKESLKNCKG ALWVHTASIG EFNTFLPILK ELKREHRILL TYFSPRAREY
70 80 90 100 110 120
LKTKSDFYDC LHPLPLDNPF SVKRFEELSK PKALIVVERE FWPSLIIFTK VPKILVNAYA
130 140 150 160 170 180
KGSLIEKILS KKFDLIIMRT QEDVEKFKTF GAKRVFSCGN LKFICQKGKG IKLKGEFIVA
190 200 210 220 230 240
GSIHTGEVEI ILKAFKEIKK TYSSLKLILV PRHIENAKIF EKKARDFGFK TSFFENLEGD
250 260 270 280 290 300
VILVDRFGIL KELYPVGKIA IVGGTFVNIG GHNLLEPTCW GIPVIYGPYT HKVNDLKEFL
310 320 330 340 350
EKEGAGFEVK NETELVTKLT ELLSVKKEIK VEEKSREIKG CYLEKLREFL RGL