ID A0A1Y1CM83_9BACT Unreviewed; 911 AA.
AC A0A1Y1CM83;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=ALGA_2750 {ECO:0000313|EMBL:BAX81062.1};
OS Labilibaculum antarcticum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Labilibaculum.
OX NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX81062.1, ECO:0000313|Proteomes:UP000218267};
RN [1] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:BAX81062.1, ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|EMBL:BAX81062.1,
RC ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 39:1-2(2018).
RN [3] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL Antonie Van Leeuwenhoek 113:349-355(2020).
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; AP018042; BAX81062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1CM83; -.
DR KEGG; mbas:ALGA_2750; -.
DR Proteomes; UP000218267; Chromosome.
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; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAX81062.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:BAX81062.1}.
FT DOMAIN 205..235
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 427..497
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 545..591
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 616..670
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 688..911
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 911 AA; 104220 MW; C270CD450166C810 CRC64;
MKLDGESIEV FAKSEMSENP YKVGDREKLY GLYCNTVIET HNKLLVPNAL KDINWMNNPD
VKLGMIAYLG FPIYLPNNSI FGTICVLDNN ENCFPKEIEQ LLEQIKEIIE LDIEGYLAFE
SKSIKLETKV LEQIQIIDQA KTPRQKLSNK VKKEHKIQES ITNNNQQLID KLVEGESKDA
DLFNKLNSAI VMFSPVFGSE GELIDATYLD MNPMNEQLIG YKKEEVIGKS ILEIFPETSP
KWFRTFGPIF KGKSNVNFEM FHKPLGKHFS VNAFPIDDGS FCVNYFDISK QVILKENSKE
NQLLLSSIFN RINVAIVLFK PIFNQIHDLI DLEYIDMNPL NEQIMDFKLA DVKGKTVLEL
FPNTNKEFFG YFNTSIQQKR IVPFNFKIDS SKKFYHSNAF MLDDNRMVYT CYDITEQILA
TKKMEEREKR HKAIFNNSSS SIVLIDSDSG AILDGNDALV RYTGYSKKTL LKMNLKQIST
SSEEEIQKQL YLAKQNKKHF DFKHTLASGE IRNIEAYVGQ IEMNGKMILH CTVHDITDKK
NALQDVLKLS NAVEQSPASI IITDTHGNIE YTNPKNCEIT GYSAENLKGK NPRILKSGKL
AEHTYKDLWN TILAGGKWEG EFYNRKKNGN YYWEHASISP IKNEEGTTIN FMKIGKDISE
QKKIQSELRK AKFRAEENDR LKTAFLANLS HEIRTPLNGI MGFTDLILHE ETPDDAKKDY
QNIVKESGEQ LLMIINDLVN ISQIEAGELN IKLSHFSATD LLDEILLFYK PEVSKKGLEI
QIVKINCQVI KSGINCMLFS DRKRLRQVFD NLIKNAIKFT QKGTITLGIE CRDYTVLFTI
QDTGIGISKE NQKLIFDRFR QVEEHFTRHY GGNGLGLSIS KEITELLGGE LWVESDLGKG
SKFSFTVANN S
//