ID A0A2K4DS28_9STAP Unreviewed; 188 AA. AC A0A2K4DS28; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 25-APR-2018, entry version 2. DE RecName: Full=Accessory gene regulator protein B {ECO:0000256|HAMAP-Rule:MF_00784}; DE EC=3.4.-.- {ECO:0000256|HAMAP-Rule:MF_00784}; GN Name=agrB {ECO:0000256|HAMAP-Rule:MF_00784}; GN ORFNames=CD147_02520 {ECO:0000313|EMBL:PNZ89630.1}; OS Staphylococcus devriesei. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=586733 {ECO:0000313|EMBL:PNZ89630.1}; RN [1] {ECO:0000313|EMBL:PNZ89630.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CCUG 58238 {ECO:0000313|EMBL:PNZ89630.1}; RA Cole K., Golubchik T., Russell J., Foster D., Llewelyn M., Wilson D., RA Crook D., Paul J.; RT "Draft genome sequences of 64 type strains of genus Staph aureus."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Essential for the production of a quorum sensing system CC signal molecule, the autoinducing peptide (AIP). This quorum CC sensing system is responsible for the regulation of the expression CC of virulence factor genes. Involved in the proteolytic processing CC of AgrD, the precursor of AIP. {ECO:0000256|HAMAP-Rule:MF_00784}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00784}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00784}. CC -!- SIMILARITY: Belongs to the AgrB family. {ECO:0000256|HAMAP- CC Rule:MF_00784}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PNZ89630.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PPRG01000015; PNZ89630.1; -; Genomic_DNA. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR HAMAP; MF_00784; AgrB; 1. DR InterPro; IPR006741; AgrB. DR Pfam; PF04647; AgrB; 1. DR SMART; SM00793; AgrB; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00784}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00784}; KW Kinase {ECO:0000313|EMBL:PNZ89630.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00784}; KW Protease {ECO:0000256|HAMAP-Rule:MF_00784}; KW Quorum sensing {ECO:0000256|HAMAP-Rule:MF_00784}; KW Transferase {ECO:0000313|EMBL:PNZ89630.1}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00784}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00784}; KW Virulence {ECO:0000256|HAMAP-Rule:MF_00784}. FT TRANSMEM 44 69 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00784}. FT TRANSMEM 81 102 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00784}. FT TRANSMEM 108 127 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00784}. FT TRANSMEM 143 160 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00784}. FT TRANSMEM 166 183 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00784}. SQ SEQUENCE 188 AA; 21122 MW; 9F6B1872C718B1E7 CRC64; MKAIDKKIEQ FAYYLQKRNN LDHIQFLKVR LGLQVAVSNI AKTIVTYGAA LIFHTFLYTL ITHVCYFLVR HYAHGAHAKS SLLCHIQNLI LFVALPAMVV FFQVNVGIMY TVALLGLMLI VILAPSATKK QPIPPPLVRR KKVLAIILTV FLIIISFVVS EPFKQLILLG VALESATLLP IFIPKEDN //