ID U4T3L9_9GAMM Unreviewed; 1153 AA.
AC U4T3L9;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=M917_1652 {ECO:0000313|EMBL:ERL55395.1};
OS Psychrobacter aquaticus CMS 56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1354303 {ECO:0000313|EMBL:ERL55395.1, ECO:0000313|Proteomes:UP000016761};
RN [1] {ECO:0000313|EMBL:ERL55395.1, ECO:0000313|Proteomes:UP000016761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 56 {ECO:0000313|EMBL:ERL55395.1,
RC ECO:0000313|Proteomes:UP000016761};
RX PubMed=24201199;
RA Reddy G.S., Ara S., Singh A., Kumar Pinnaka A., Shivaji S.;
RT "Draft Genome Sequence of Psychrobacter aquaticus Strain CMS 56T, Isolated
RT from a Cyanobacterial Mat Sample Collected from Water Bodies in the McMurdo
RT Dry Valley Region of Antarctica.";
RL Genome Announc. 1:e00918-13(2013).
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:ERL55395.1}.
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DR EMBL; AUSW01000030; ERL55395.1; -; Genomic_DNA.
DR RefSeq; WP_021814288.1; NZ_AUSW01000030.1.
DR AlphaFoldDB; U4T3L9; -.
DR STRING; 1354303.M917_1652; -.
DR PATRIC; fig|1354303.4.peg.1628; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9797243at2; -.
DR Proteomes; UP000016761; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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 PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:ERL55395.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ERL55395.1};
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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..531
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 686..857
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1034..1134
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 732..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 251..278
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 732..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 789
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1073
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1153 AA; 129650 MW; E8C92E54CF40CC3B CRC64;
MAHKKRFDTS SAYGQLIILV FLPICVLAAV GGILVFYETM RASNSEQEVL AEAVLIRYTP
AIAELIPELL EQARNDVDVS ANDTSKTEGA QLKGIQDKLN RMQSEQHVQR IAIINESNQV
LAAVGYGRDE AWPLIGLQEK FLSQRPTPIG TAYGSVLGEF KGQRMWLLVD MDNEPLYIAR
YRIAMALVIT GLFTILILLL SLNIYSKRWI APIYELRLQL QRTHVDNLYH PIPVESDGEL
NLLQQDLVKT LRRLHRSFQE LKDHAEQTED DLRLAFDEME MQNISIRNAR DAAISTSQAK
SAFLANISHE LRTPLNSIDG FINLLARHGE LNPEQDLYVQ TIRKSSAHLL ALVNDVLDFS
KIEAGKLVLD RHEFDLYDTI YDVVDMLSPV SAEKGLRMAV LFYNDVPMRI NGDALRLKQV
LTNIVGNAIK FTDSGDVVVR VSLDDHRDNY LMISVQDSGK GISLADQKML FQSFSQGDPS
ITRQYGGTGL GLVISKQLTR LMGGDIGFHD NAQENIANQG ATFWFRMPAH VDVLEAATGQ
TIELPVLAPL ASATDEFNVL VWINHTASIQ VLKASLQYLP IKLTQANSLP GVLESLKEHG
NYWDWVIVDD DTQDDMMALL KQIRLHYQGK LAVFGYQVAA DQALLNRYHA NILYEPLDKR
QLYAMLDTQS RSVPKSMQEP RWKGVTVLAV DDHLPNLLVL DALLSELGIQ VITASSGFDA
IEIISKQQTK NIKTTKNDKQ SLSNKTQLSK AETRDEVSKK ANSTLYEEAS VDDKGAAQDK
NNIDLIFMDI QMPRMSGHEA ARQIRNIEND DSRIPIIALT AHGLADERDK LIASGINDYV
GKPISQPQLL QVLQKWLGRT TTTAQLALPD TTLHSVDPQA IDLNDLQATV LQNSDAENYS
TWPSDSTVIA YPMVKNHESN HTSASDITNQ PKITRPLSLK KIRDDYLRDS QPREDYRRET
PRNTQPRYES IRLQKQGSSS SLHPPKNSVD SSHDEVTTDA SGATHLSRNH LSVSYINTLD
ILDWQDALTR SANKPDLAAK LIIMMLDTID NEKQALTQAW ETRDRHMLAQ IAHRILGGSR
YTGVPQLRQA SQDLEDKCLL NVQHTTPAQF AMLEPYYDSL LIALNNLQTL DLSFYPQLNY
HRLSENDMTW KMI
//