ID A0A1Y5JTU8_9GAMM Unreviewed; 921 AA.
AC A0A1Y5JTU8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B5G52_16705 {ECO:0000313|EMBL:OUS69535.1};
OS Pseudoalteromonas sp. A601.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1967839 {ECO:0000313|EMBL:OUS69535.1, ECO:0000313|Proteomes:UP000196208};
RN [1] {ECO:0000313|EMBL:OUS69535.1, ECO:0000313|Proteomes:UP000196208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A601 {ECO:0000313|EMBL:OUS69535.1,
RC ECO:0000313|Proteomes:UP000196208};
RA Cheng Y., Li J.G., Liu H., Han W.J.;
RT "Draft Genome of a Polysaccharide-Degrading Marine Bacterium
RT Pseudoalteromonas sp. A601.";
RL Submitted (MAR-2017) 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 inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:OUS69535.1}.
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DR EMBL; MXQF01000024; OUS69535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5JTU8; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000196208; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:OUS69535.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:OUS69535.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 296..511
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 671..787
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 825..921
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 785..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 720
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 864
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 921 AA; 103153 MW; 73F452DA476D8F11 CRC64;
MTKLGLRDSV LTLTLIPTVL IGLLLGGYFT INRYFELDEI LYQQGTTISE PLSIAIEQPL
LVKNKQLLNR LISHTHNKHS PAIKTIAIFD VNEQLVLTSN YHRDFDDLML SEHLSTNKTT
KVVQSSDFIT FYTPIINHST PEAHWNDTAF QTSIGTVIVQ LNKDQAIIGQ QQALLVSGIV
IIFALLLAVI LAIRLSRMFM TPLNKLVLAT DKLTEGKRDT GLNTPMMGEF ELLRQGLNTI
SDTMVMQKDE MQKHIDQATS DLRESLEMYE TQNIQLNIAK TDAQDANRVK SDFLAKMSHE
LRTPLNGVIG FTRQLHKTPL NKHQKDYLDT IELSANSLMT IISDILDFSK LEAGAMELES
IQFQLRDNIN EVLTLLAPSA DEKQLELSIY INSQVPDNIT GDPTRFKQVL INLISNAIKF
TEKGAIKVDV GHRLLDEERT SILVSITDTG VGIPMDKQDA LFTPFGQADS SITRKFGGTG
LGLIITKHIV EAMGGRITLN SAPGHGTCFT FNGVFNLPSH GYNSDLPSKS LANKRILYLE
PHEHTHHAVL SLLNEWDTQV TGCFSEECFL EEINKDFNYD ICIIGHVASV DEMQRLKSYI
KAARNSTDYL YLMLNTVSHS MREAYIGSGA DACLSKPLNH RKLCEVLAAP YRLDHPVHNI
EENDEKLLPL KVLVVDDNDA NLKLICTLLE EQIEIIDTAH NGSQAYSLSK SHKYDIIFMD
IQMPIMDGIT ACKLIRESSL NEDTPIIAVT AHALAGEKEQ LIKDGFKGYL TKPIDEDMLK
QIISDHSPKS PLKRDKSRQE QTHYEPPFNS SSLDWPLALQ RAGGKHELAL EMLNMLLLSV
PETLRLLDEA IQSQDCEHVL SIIHKFHGAC CYTGVPKLKN LAEALETALK SDCELSHIEP
ELFELQDELE NLIKDAGMAD D
//
