ID G0J8D2_CYCMS Unreviewed; 1375 AA.
AC G0J8D2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cycma_5048 {ECO:0000313|EMBL:AEL28732.1};
OS Cyclobacterium marinum (strain ATCC 25205 / DSM 745 / LMG 13164 / NCIMB
OS 1802) (Flectobacillus marinus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=880070 {ECO:0000313|EMBL:AEL28732.1, ECO:0000313|Proteomes:UP000001635};
RN [1] {ECO:0000313|Proteomes:UP000001635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25205 / DSM 745 / LMG 13164 / NCIMB 1802
RC {ECO:0000313|Proteomes:UP000001635};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Cyclobacterium marinum DSM 745.";
RL Submitted (JUL-2011) 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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP002955; AEL28732.1; -; Genomic_DNA.
DR RefSeq; WP_014023011.1; NC_015914.1.
DR STRING; 880070.Cycma_5048; -.
DR KEGG; cmr:Cycma_5048; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_255982_0_0_10; -.
DR OrthoDB; 9811889at2; -.
DR Proteomes; UP000001635; Chromosome.
DR GO; GO:0005524; F:ATP binding; 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; cd00130; PAS; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR016132; Phyto_chromo_attachment.
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; 3.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF55781; GAF domain-like; 1.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEL28732.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001635};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..236
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 289..359
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 488..539
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 559..701
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 735..957
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 972..1091
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1116..1234
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1278..1370
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1021
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1167
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1317
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1375 AA; 156099 MW; 22319DB2EB9744D2 CRC64;
MKKNISDNNT ENTGHNKKMN PENNSRQQIS SKIVALAQKL SACNHSFLGV LQDEVICILS
ASGIETNQNI PKNDPFYYFL ENIKEFKAIH EIHNEKELTG SKYLNEIGDI KYLAILPIIN
KDNSTLGFIV VFNEEIPAEN LNVAENLDLL YPQAKEVLIA QAGELEDQIL SKAMVLSQDL
ITILGSDGKI IKVNKAFKTL LGYDEKEISD KPVLDYIHPD DVKSTMKQIQ LLIKGEEQTA
IFYHRLKCHN GEYKTFAWRA TGDLENNLVF AIGRDISEET KNKERLLASE EKFRSFFENS
QGLMLTHDME GNFLSFNSYG ARLLGYTVEE MLTKKLWDII PSKFRFEIDD YIKEIKENGE
AQGLMTTFQA NGQLKVWLYS NKLEKDHFGK QYVIGNSIDI TERLRLEKRI QNAKEFLNQT
HAMAKIGGWK YDVEKQSINW TDITKSIFGV SDDYIPDLES GINFYKEGES RDKVKEVIDL
AMHYGKPWDE RLKIINDKGK EIWVRTLGEA HIEDGKCLYL SGTIQDIDEE VKKEKQLIQK
EQMLGAISKA TDELLSNNKL YEAIPNSLEI IGKSVGVDRI YYFENSIGDE GEKYTSQRFE
WSNDSVEAQI NNPDLQNIPL EAFGDFVFPM ENNEVFMAII SNLPDESETK QFLDNQNIKS
ILTIPIFTEN GFWGFIGYDD CTNEREWSKA ELSLLRSFAN SISNAIDRNI LEKNLIESKE
IAEKASLAKS EFLANMSHEI RTPLNGIIGF TDLLVKTELD ETQSQYINIV NQSAVSLLNI
INDILDFSKI EAGKLELEII KSDIFELSGQ ATDVVSYQAQ QKGVEMLLNI EKSLPRFIQV
DDIRLKQILI NLLGNAVKFT DKGEIELKIH TLNKIDKNKR VIRFEVRDTG IGISEEYQKR
IFDAFMQEDG STTKKYGGTG LGLTISNKLL SMMGSELQLN SKLNEGSTFY FDLELVTEEG
ELEPLADYPL NNVLVVDDNS NNRYILKEIF SLNDIKVDEA ENGFEALKQI ESNDYDVVLM
DLNMPYMDGI ETTKKIRENF TNKKSQVPIL LLHSSAEDDY ILKQCKELSI NRRISKPIKN
KELFEALSKL QPPKQSTSRG TVEQADTGKK ETVGARVLIA EDNSINMFLA KTIVLKVSPK
VEIFEATNGL DAYEMATEFL PDIILMDIQM PIMSGHEATK KLKENPKTKD IPIIAITAGN
IKGEKEKCMA SGMSDFVPKP IVEKNIIYIF DRWLNTKETE KTSEEEELNE MPAEKDGAIT
EQKDHFDVDK VKEFLGDEPE IIKEVLKLTI HELEQSKTVL ANHYTNKDLG GLSSEGHKLK
GSALTAGLGE VYKTALALEE MKTLDLPLAK KLIDSFDAEY NLVVDLINDY IARGN
//
