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Database: UniProt
Entry: U4T3L9_9GAMM
LinkDB: U4T3L9_9GAMM
Original site: U4T3L9_9GAMM 
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
//
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