ID F5T2V2_9GAMM Unreviewed; 790 AA.
AC F5T2V2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=MAMP_00798 {ECO:0000313|EMBL:EGL53313.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL53313.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL53313.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
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:EGL53313.1}.
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DR EMBL; AFIG01000003; EGL53313.1; -; Genomic_DNA.
DR RefSeq; WP_007146563.1; NZ_AFIG01000003.1.
DR AlphaFoldDB; F5T2V2; -.
DR STRING; 1026882.MAMP_00798; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9792854at2; -.
DR Proteomes; UP000003544; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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; 3.30.450.20; PAS 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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGL53313.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003544};
KW Transferase {ECO:0000313|EMBL:EGL53313.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..345
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 355..405
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 423..641
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 667..784
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 717
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 790 AA; 89597 MW; 90D59B330FFEA937 CRC64;
MQQDLYQLVD GSLKATITNE GYRDYKLFNL NGELILSGIS GFAKPEQNIT LPDNILAALS
KKDVYTSHPF MPSSVWQSTL RHQYPLPTML FIAPIHDWAG KTVAFFAFEI NPDKLFNPAF
HENQVGQTGQ AYAIDEQGRM LTQSKFTNQL IRAGLIDASN PLTELKLEVR DPGFDLLESP
DKKVKSPMPL TLMAKSLTQH KTGVNLKGYR DYRGVKVIGS WRWDEQLNMG IVTETEVSEV
YKLYRSLLFS VIVSIVFIIF MTAFGTYFYR RSTQQQIVSL QQRDAIIKQT DDGFVTIDDQ
GRITMVNPAI CLLFGYQEAE LIGQPVSILI DEEQRHKHDN YLKQADIHEP KIIHRTRSLS
ATRKDRSQFP IELNVSPMQF GHRKFYIGVI RDISERYQYQ QELIKAMQQA EHANQAKSEF
LAKMSHELRT PLNAIIGFSQ LLQMDKLNDD QRESVSMIES SGNHLLSLIN EVLDLSRIES
GHMSVSVEDV ELKPLIDHIL PFIQTHLKTL NLSITESYPK QTTSLFVRAD HVKLKQVLLN
LLSNAAKYNR PNGSIEIIIS HTDNQSTRIA IKDTGYGIDE KLQQRLFEPF DRLDKDTSDI
QGTGIGLVIS RELIKLMNGR FGFESEPDKG STFWIELQRS SANNSSILSP ADSEPDQLSG
AQIKHIKILC IEDNPTNLNL MQRVFKQYPQ FALLTAADAE AGLELARQFE PQVILMDINL
PGKSGFEALK DLKRSAITRD IKTIALSANA MPQDIDKGLK AGFDYYLTKP LNFELLIETI
NQAIEKAIKH
//
