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Database: UniProt
Entry: A0A3S2XPM2_9BURK
LinkDB: A0A3S2XPM2_9BURK
Original site: A0A3S2XPM2_9BURK 
ID   A0A3S2XPM2_9BURK        Unreviewed;      1361 AA.
AC   A0A3S2XPM2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-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=EOD73_14945 {ECO:0000313|EMBL:RVT83856.1};
OS   Inhella crocodyli.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Inhella.
OX   NCBI_TaxID=2499851 {ECO:0000313|EMBL:RVT83856.1, ECO:0000313|Proteomes:UP000288587};
RN   [1] {ECO:0000313|EMBL:RVT83856.1, ECO:0000313|Proteomes:UP000288587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCP-18 {ECO:0000313|EMBL:RVT83856.1,
RC   ECO:0000313|Proteomes:UP000288587};
RA   Chen W.-M.;
RL   Submitted (JAN-2019) 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:RVT83856.1}.
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DR   EMBL; SACM01000004; RVT83856.1; -; Genomic_DNA.
DR   OrthoDB; 5290456at2; -.
DR   Proteomes; UP000288587; Unassembled WGS sequence.
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; cd00130; PAS; 2.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
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   NCBIfam; TIGR00229; sensory_box; 2.
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; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:RVT83856.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000288587};
KW   Transferase {ECO:0000313|EMBL:RVT83856.1}.
FT   DOMAIN          350..426
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          429..481
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          621..842
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          860..981
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1009..1126
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1175..1270
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   REGION          1128..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         914
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1059
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1214
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1361 AA;  145968 MW;  A7522ACD1A5A72E4 CRC64;
     MARSDPAGPL TLSVSARLGV LLAALGLALA ALAGYAQWVI GDHTRLLQAR VEREALALEQ
     RTLTGQSMGA VALAGRLNLD LMEAASAPGL EAAPAPSLVS ALQTLAASVQ ADQAYLANRA
     GQVVAQSGTI DGLERGMNVA FRHYFQQALS GQPSASIAVD ASSAGRHSYI AAPVYRNREA
     QSTADIVGVV VARERSEEVD RQLSHWPHTL GLLLSPEHVV MAGNRSDWLL RHVGELSAEK
     QRRFASNHLY GKRGSEIQAA QALPDFLGGG LHWMDGALYL AAASPVNFNH RLGAWKLVYL
     GELSAVLSPY TLGAVGLLTF LTSAVLGHLV LRRRADQALR AQQQRALALS QAQVQAMVQN
     LPGVVFRSEA QPPWRLDFLS PAVQDLSGYP AADFLGDSAP RRLVDLIHPD DAPAWQATLR
     SGLATQQGFG HELRVVHRDG SARWALFRCM PTADETGQAR HLDGMLFDIH ERKQAEAALR
     DNEARLRDLL DLAPVGCSIN TREGRPAFSN RRLAELLGRD RDDLTQLNTA DYWAEPSERQ
     AFVDRLWADG RVEGYRARFR RADGQAFTVL LTSSIENILG ADHIVSWSYD ITQLEAAEQA
     ICQARDAAEA ATRAKSDFLA NMSHEIRTPM NAIIGMSHLA LQAPLERKPR HYIEKVHLAA
     NNLLGIINDI LDFSKIEAGK LDLESVPFQL EDLLDGFANL VGFKAQEKRL DLLVRLDPAT
     PTALVGDPLR LGQVLTNLGN NAVKFTAQGE IELGITTQNR DDESVELHLW VRDSGIGLSP
     EQQGRLFQSF SQADSSTTRK YGGTGLGLAI SKNLVERMQG RIWVESQAGQ GATFHFTVRL
     GLQAHSPSAA APSNALTGLR VLVVDDSAHS RDILMSTLQA FGMTADGASN GDEAQALAQA
     AEDNGRPYAL MLMDRDMPGQ DGIAALQVLQ AAPHCPPAWL IASGDAEQAR EAASQVGVTL
     AGVLVRPVTP SHLFEAVGRS TGGHAPVATR RWQRAELAQQ ARQHLRGARL LLVEDNDMNQ
     ELALELLRGA GIEVVLAENG QEALDRLAAE SPFDGVLMDC QMPVMDGYTA TRTLRQNPAW
     QQLPVIAMTA NAMAGDREKV LAAGMNDHIA KPLDVGAMFA TLARWVTPPR PASEPADTTP
     TELDAPPPEN DGFDPSTLAF DGLDPQAGLR IAAHNSALYL RLLRRFQQGT RTFVHDFVGA
     QAQPDAEAPA RLAHTLKSTA GHIGAHALQA AAAALEATCR LPDASPAQCD AALAAVQVPL
     EALLATLDAR LPAPAAAAPS AASHDWQASS AQQQQLVRLR ALLQDSEAEA TDALDALLDS
     CAGSPWASAL QQAQQALAGY DFDAALQALQ GLSSPHNGPT G
//
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