ID D0LG19_HALO1 Unreviewed; 2107 AA.
AC D0LG19;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Hoch_2076 {ECO:0000313|EMBL:ACY14621.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY14621.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY14621.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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; CP001804; ACY14621.1; -; Genomic_DNA.
DR RefSeq; WP_012827229.1; NC_013440.1.
DR STRING; 502025.Hoch_2076; -.
DR KEGG; hoh:Hoch_2076; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0840; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_3_0_7; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 10.
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; 1.20.120.1530; -; 8.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
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; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 10.
DR Pfam; PF18947; HAMP_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 12.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 7.
DR PROSITE; PS50885; HAMP; 12.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACY14621.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..158
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 198..250
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 290..342
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 382..434
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 474..526
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 566..618
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 658..710
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 750..802
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 842..894
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 934..986
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1026..1078
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1118..1170
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1415..1645
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1719..1832
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1841..1957
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1988..2105
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1362..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1768
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1890
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 2038
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2107 AA; 229535 MW; 861630BF14CFE046 CRC64;
MATSRVKSNP EELTKKQILS ALRAFKRGEF STRLPDDLIG IDGQICETFN DILTLAETLS
TEVGVLRGDV GSDGHVRRRL RRNGARGGWA VYVTSVNELI DDLTNHLSEI AAVVAAVARG
DLTQRIEIEG SDEPLQGAFL RYARTVNDMV DRLAAFSSEV TRVALDVGVE GKLGAQARIK
GVEGTWKELT DSVNSMASNL TSQVREIARV TTAVAQGDLT KTINIEVRGE LLALKNTINT
MVDQLGSFAD EVTRVAREVG TEGMLGGQAQ VRGVSGVWRE LTENVNSMAN NLTLQVRNIA
EVATAIARGD LSRKITVEVA GELLELKQTI NTMVDQLGSF AAEVTRMARE VGTEGVLGGQ
AEVGEISGVW RELTENVNSM ANNLTQQVRN IAEVTTAIAE GDLSRKITVD ARGEILALKN
TVNTTVDKLN SFSAEVTRVA RLVGTEGTLG VQAEVKGVSG IWKELTDNVN LMGRNLTDQV
RDIANVTTAV ANGDLSKKIT VEVKGEILAL KNTINNMVDS LGSFADEVTR LAREVGTEGV
LGGQATVVGV SGIWKELTDN VNSMTNDLTN QVRSIAEVAA AVASGELSKK IAVDARGEML
DLKNSINTMV DQLSLFADEV TRMSREVGVE GKLGGQAEVE GARGIWKELT DNVNLMGRNL
TNQVRDIAEV TTAVARGDLT RKIAVDARGE ILELKNTINT MVDQLGSFAD EVTRLASEVG
VEGRLGGQAD VRGVSGTWRH LTDAVNSMAR NLTDQVRNIA QVATAIAQGD LQKKIVVDAR
GEILELKNTI NTMVGQLSSF AEQVTRVARE VGTEGKLGGQ ASVEGVSGIW KELTDNVNLM
ASNLTNQMRD ISQVATAIAQ GDLGQKVTVE TRGELLELKN TINTMVDQLG SFADEVTRVA
REVGVEGRLG GQADVRGVSG IWKELTDNVN LMGRNLTDQV RDIADVTTAV ANGDLSKKIT
VAVKGEILAL KNTINSMVDS LGSFADEVTR LAREVGTEGT LGGQAEVRGV SGIWKELTDN
VNLMARNLTE QVRGIARVVT AVANGDLKQQ LMLEARGEIA TLVDTINDMI VTLSRFADQV
SGVARDVGVE GRLGGQAVVP GAAGIWRDLT NNVNELAGNL TRQVRAIGDV ATAVTKGELT
QSIDVEARGE VAILKDNLNQ MIQTLAQTTR VNQEQDWLKT NLTRFTRMLQ GQRDLLTVAR
QVLSELAPVV DAQHGGFYMV SPGDDEPTLR LFASYAYMER KHVANQFGFG EGLVGQAALE
RKRILVTSLP DDYVQITSGL GEARPRAVVV VPVVFEEEVK GVIELGSFQI FSSIQLAFLD
ELIESLGIVV ATIEATMRTD ELLRQSRNLA EELTTQQEEL QQTNEELEEK ARQLTEQKSE
VERKNQQVEL ARQELEEKAE QLALTSRYKS EFLANMSHEL RTPLNSLLIL SRQLATNRDN
NLSDKQVEYA STIHQSGADL LSLINEILDL AKIESGTMAV EVSSVSFSQL SDYVERLFRQ
VADESGVVYQ IECADELPAA IETDEQRLRQ VLRNLLSNAF KFTKKGEVML RMSTVKPEAD
GDYGDEPFLV AFSVSDTGIG IPKDKQRIIF EAFQQADGGT SRRFGGTGLG LSISREIAEL
LGGELDVESE PGRGSTFTLY LPPSYRGPAR ARGASEIKRS GPKPRVAELP GAALKALLPT
RAASEAGHAS DDDESEMPQH ISTRSVADDR KHISAGDRVL LIIEDDDVFA RTLLDAVRER
GFRGLVALSG NEGLAVAKSY KPDAITLDLR LPDMDGWVVL DRLKHDSETG HIPVHIISAA
ADERRGLENG ALAFLNKPVG PEALDVALSD IESFLDRRVK RVLIVEDDDV QRRALVELID
GEDVSTEAVG SAEAALQALE SGTFDCMIID LKLPEMSGDE LIEKFKERPA FRRMPVIVYT
GKELSEGDEI SLRRLAETII VKDVRSPERL LAETMLFLHR VESDLPESKQ RMLRNRFAEG
DPALADKKIL VVDDDVRNIF AITTILEQHL MDVVYAENGR EALDQLDRNP DIDIVLMDIM
MPEMDGYEAT RRIRSDGRYG RLPVIALTAK AMKGDRDKCI EAGASDYITK PVDPDQLISL
LRVWLYR
//
