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Database: UniProt
Entry: A0A1I3ML88_9PLAN
LinkDB: A0A1I3ML88_9PLAN
Original site: A0A1I3ML88_9PLAN 
ID   A0A1I3ML88_9PLAN        Unreviewed;       869 AA.
AC   A0A1I3ML88;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05421753_11436 {ECO:0000313|EMBL:SFI97560.1};
OS   Planctomicrobium piriforme.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomicrobium.
OX   NCBI_TaxID=1576369 {ECO:0000313|EMBL:SFI97560.1, ECO:0000313|Proteomes:UP000199518};
RN   [1] {ECO:0000313|Proteomes:UP000199518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26348 {ECO:0000313|Proteomes:UP000199518};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOQD01000014; SFI97560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3ML88; -.
DR   STRING; 1576369.SAMN05421753_11436; -.
DR   OrthoDB; 9762493at2; -.
DR   Proteomes; UP000199518; 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; cd00156; REC; 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; 3.30.450.350; CHASE domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
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; PF03924; CHASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM01079; CHASE; 1.
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; PS50839; CHASE; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SFI97560.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199518};
KW   Transferase {ECO:0000313|EMBL:SFI97560.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..220
FT                   /note="CHASE"
FT                   /evidence="ECO:0000259|PROSITE:PS50839"
FT   DOMAIN          358..579
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          599..720
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          745..863
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          331..358
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         653
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         794
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   869 AA;  94753 MW;  A85077D96FCE06D4 CRC64;
     MQHTSSATVG KDFLRVSAPL VTLLIGCGVA LLLTLMVWQF GESRRQAEIQ ALAVQNARDI
     QRMVDVQLEA VESIRALYAA SVSVEPEEFS SFTKSLLQRR KGIRILAWAP VETASGEAAF
     PVRVLEPAEN SSDWTRVDLM QLPGCRAAID AAIAIGSPVV TDVLPLKMGA KETIACLVLS
     PIYENRQPVD SAAERREHLQ GVVVGVCALS DLIGAALPPL EEDGLAFVLT DQPFTKTPPN
     KPMFESRGWS AAAANQTRAP ESMLAIDVAG RQWWLAHRPT ARFKPSQPAW EHWAVLIGGL
     WITSLLAAYL YSIRGRTRRI EAMVTERTSE LAAANAALSR AKETAEAANR AKSEFLANMS
     HEIRTPMNGV IGMTDLALGT SLTPEQREYM ELVKCSADYL LSVINDILDF SKIEAGKMDL
     EAIPFSLHEN LDKTVASLAM RAHAKKLELA CHILHDVPDG LTGDPGRVRQ VLINLLGNAI
     KFTEKGEIVL KVELVSRTSD AATLRFSVRD TGIGIPPEKR DRLFKAFSQV DSSTTRKYGG
     TGLGLAISAR LVKLMDGQLD VQSTPGEGST FFFTAKFELA PLDSLPAVQL EPESLHGLQI
     LAVDDNATNR RILCELLTSW GMRPAVAEGG VAALQELERA RNAGQPYALV MTDNMMPDMS
     GFELVAEIQR RPELSAPLLM MLSSADRYED AQRCKEMGIA AYTTKPIRQS DLLNAIIRTL
     DGKPRPCLAA PPTKAEAGKA PHSLRLLLAE DGLVNQKLAV RLLEKRGHTV EVAPNGIATL
     AALDRAEFDA VLMDVEMPDM DGLEATATIR QRERKTGRHV PIIAMTANAM QGDRERCLNA
     GMDEYLSKPL NPAELFRIVE ALAGHAVVR
//
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