ID A0A5N0FP73_ACIBA Unreviewed; 357 AA. AC A0A5N0FP73; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 27-NOV-2024, entry version 21. DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438}; DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438}; GN Name=adeS {ECO:0000313|EMBL:MQZ69596.1}; GN ORFNames=F4T85_14565 {ECO:0000313|EMBL:MQZ69596.1}; OS Acinetobacter baumannii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:MQZ69596.1, ECO:0000313|Proteomes:UP000420346}; RN [1] {ECO:0000313|EMBL:MQZ69596.1, ECO:0000313|Proteomes:UP000420346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMA26 {ECO:0000313|EMBL:MQZ69596.1, RC ECO:0000313|Proteomes:UP000420346}; RA Maria R.S., Adams M.D.; RT "Distinct mechanisms of dissemination of NDM-1 metallo-beta-betalactamase RT in Acinetobacter species spp. in Argentina."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MQZ69596.1}. 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; VYTH01000023; MQZ69596.1; -; Genomic_DNA. DR RefSeq; WP_046882653.1; NZ_WJNS01000010.1. DR AlphaFoldDB; A0A5N0FP73; -. DR Proteomes; UP000420346; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR CDD; cd06225; HAMP; 1. DR CDD; cd00082; HisKA; 1. DR FunFam; 3.30.565.10:FF:000006; Sensor histidine kinase WalK; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 6.10.340.10; -; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR InterPro; IPR050398; Bact_Sensor_His_Kinase. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P_dom. DR InterPro; IPR036097; HisK_dim/P_sf. DR InterPro; IPR004358; Sig_transdc_His_kin-like_C. DR PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1. DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1. DR Pfam; PF00672; HAMP; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF00512; HisKA; 1. DR PRINTS; PR00344; BCTRLSENSOR. DR SMART; SM00304; HAMP; 1. DR SMART; SM00387; HATPase_c; 1. DR SMART; SM00388; HisKA; 1. DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF158472; HAMP domain-like; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR PROSITE; PS50885; HAMP; 1. DR PROSITE; PS50109; HIS_KIN; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:MQZ69596.1}; KW Membrane {ECO:0000256|ARBA:ARBA00022989}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. SQ SEQUENCE 357 AA; 40374 MW; D83ADAB9155B7704 CRC64; MKSKLGISKQ LFIALTIVNL SVTLFSVVLG YVIYNYAIEK GWISLSSFQQ EDWTSFHFVD WIWLATVIFC GCIISLVIGM RLAKRFIVPI NFLAEAAKKI SHGDLSARAY DNRIHSAEMS ELLYNFNDMA QKLEVSVKNA QVWNAAIAHD LRTPITILQG RLQGIIDGVF KPDEVLFKSL LNQVEGLSYL VEDLRTLSLV ENQQLRLNYE LFDFKAVVEK VLKAFEDRLD QAKLIPELDL TSTPVYCDRR RIEQVLIALI DNAIRYSNAG KLKISSEVVS QNWILKIEDE GPGIATEFQD DLFKPFFRLE ESRNKEFGGT GLGLAVVHAI IVALKGTIQY SNQGSKSVFT IKIPMNN //