ID A0A1T1ICA5_9PSED Unreviewed; 929 AA.
AC A0A1T1ICA5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MF4836_06365 {ECO:0000313|EMBL:OOV99854.1};
OS Pseudomonas sp. MF4836.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV99854.1, ECO:0000313|Proteomes:UP000190183};
RN [1] {ECO:0000313|Proteomes:UP000190183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA Fagerlund A.;
RT "Genome sequencing of bacteria from food industry.";
RL Submitted (FEB-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 -!- 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:OOV99854.1}.
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DR EMBL; MVOL01000002; OOV99854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1ICA5; -.
DR STRING; 1960827.MF4836_06365; -.
DR Proteomes; UP000190183; 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; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OOV99854.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:OOV99854.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..929
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010517128"
FT TRANSMEM 172..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 404..624
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 642..764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 796..915
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 696
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 845
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 929 AA; 102272 MW; EFDB3B0681D4F4D6 CRC64;
MRWLRIATGF IATLLTLLCL NTALAAQGSG WAVLLDEQAS LQLSDIRSQR YATQFSPIEL
DKLTAAEPDG ALWVRFKLHP DQHEQLLRIF APDLSQLNLY VFDGDRLIEQ VNTGTHQPQT
EKNLPSNDFM LPLPQNEKTL DVYLRLVSDH QLRPYITLQT AVMAAANQSQ TLIYGVLFGC
MAMLILHNLT RYAYTRSRSS LWLAACEVLL SLSLLMLLNL AGPWLPNWQA LQTPGAYLAL
LLTAPCGLMF AYRYFAPLGP HPLNKLLLGD ILLIILCGLL LLFVNTLPLN IITYALVALA
GLSMLLVGGY HWHKGYRPAR LFVAAMVIFN LGTLVILPAL LGLTLVAPQG LIITLLSVIC
ISGLLMSVAL GERQRSITEN RFSVSRDLAA SNAEVNAKAE FLAKISHEIR TPMNGVLGMT
ELLLGTPLSV KQRDYVQTIH SAGNELLTLI NEILDITKLE SGQIELDDVQ FDLNALIEDC
LSIFRAKAEQ QNVELISFIQ PQVPRVISGD PTRLRQALLS LLENALKKTD EGEVLIVVAL
DERSSKPRLR IAVQDSGQPM DAEERDALLH SELHSKNFLA ATRLGGNLGL VIARQLVLLM
HGEFGIKSSA NQGSTLWLTL PLDPERLEHP TSDLDGPLQG ARVLVVDDND TCRKVLVQQC
SAWGLNVSAV PSGKEALALL RTKAHLRDYF DVVLLDQNMP GMTGMQLAAK IKEDPSLNHD
ILLIMLTGIS NAPSKVIARN AGIKRILAKP VAGYTLKTTL ADELTQRNKG LVTPHYLPGN
TTAPAATPIT VPSDFRILVA EDNSISTKVI RGMLGKLNLQ PDTASNGEEA LQAMKAQRYD
LVLMDCEMPV LDGFSATQQL RAWEVGNQRV RTPVVALTAH ILAEHKERAR QAGMDGHMAK
PVELSQLREL IEHWVAQRDQ HNRSAEPAS
//
