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
//