ID V9W0A0_9RHOB Unreviewed; 749 AA.
AC V9W0A0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=METH_22480 {ECO:0000313|EMBL:AHD03598.1};
OS Leisingera methylohalidivorans DSM 14336.
OG Plasmid unnamed {ECO:0000313|EMBL:AHD03598.1}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD03598.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD03598.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD03598.1,
RC ECO:0000313|Proteomes:UP000018780};
RC PLASMID=2 {ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) 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; CP006775; AHD03598.1; -; Genomic_DNA.
DR AlphaFoldDB; V9W0A0; -.
DR KEGG; lmd:METH_22480; -.
DR PATRIC; fig|999552.6.peg.4443; -.
DR HOGENOM; CLU_000445_104_15_5; -.
DR Proteomes; UP000018780; Plasmid 2.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
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 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; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:AHD03598.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 135..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 235..455
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 474..595
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 620..739
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 528
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 669
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 749 AA; 81271 MW; CCB152DF35E577E9 CRC64;
MSLLLAASAV GLAVGHLAKR QEVQRLEEQL AEQADLTVSL LSGLMLESII VEDVPVLETG
LIEAVNRNPK IVSIQIRSPS GRLLAAANAP AVPPPDHHVI YERPIELEGA SFGTMMVEWS
TRDGEALVAA KVRQIIIWTV VPVLALSLLV LLLVHVLALR PLQMIHNRMS DALAGLRSPL
RPLPWFASRE FRALDFSVGV LEDAFAERDE REYAMEQARE AADIANRAKS EFLANMSHEI
RTPMNGVIGM AELLQDTALD EDQRMYAETI SKSGTALLTI INDILNFSKI EAGKVELNLA
PFNLQTALED VVTLLSPKAA EKGVEITLRY DPALPEIFVG DAGRIRQVIT NVAGNAVKFT
RKGYVYIDLT GRAQDGRHLL TLQVTDTGIG IEPDRTGDIF RAFEQADNAA SRNFEGTGLG
LAISARLLTL MGGSVRVRSE LGEGSVFTIE LPLQAGGHVA PARAGSPLSL AGLHGLLVDD
LELNRVMLSE RLSSWGVACT LAGSAHEGLE ILSDAQLDGR RFDFIILDYQ MPAMDGQELA
ARIRAMPGFE TVPLIVLSSV EHALTRSDCE AIGNCEFALK PVRAVQLQQV ITRVLNVQGE
KPAAVASGGG MEAPQVRRVN VLLAEDNRTN QLVVTKMLKN TPLKISVAKN GVEAVAQFQA
ERPDIVLMDM MMPEMDGLEA TAEMRRIEAE TGCGRCPIVA LTANALQTHR EKCLAAGMDD
FLSKPINKKA LIEAVSKWTC DDDLQRTGS
//
