ID M4U0X6_9GAMM Unreviewed; 784 AA.
AC M4U0X6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PCNPT3_00505 {ECO:0000313|EMBL:AGH80043.1};
OS Psychromonas sp. CNPT3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=314282 {ECO:0000313|EMBL:AGH80043.1, ECO:0000313|Proteomes:UP000010320};
RN [1] {ECO:0000313|EMBL:AGH80043.1, ECO:0000313|Proteomes:UP000010320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNPT3 {ECO:0000313|EMBL:AGH80043.1,
RC ECO:0000313|Proteomes:UP000010320};
RA Lauro F.M., Chastain R.A., Stratton T.K., Ferriera S., Johnson J.,
RA Yayanos A.A., Bartlett D.H.;
RT "The complete genome sequence of the deep-sea bacterium Psychromonas
RT CNPT2.";
RL Submitted (MAR-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004404; AGH80043.1; -; Genomic_DNA.
DR RefSeq; WP_015463925.1; NC_020802.1.
DR AlphaFoldDB; M4U0X6; -.
DR STRING; 314282.PCNPT3_00505; -.
DR KEGG; psy:PCNPT3_00505; -.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG4192; Bacteria.
DR HOGENOM; CLU_020981_0_0_6; -.
DR Proteomes; UP000010320; Chromosome.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 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; 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR017116; Sig_transdc_His_kinase_PgtB.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PIRSF; PIRSF037119; STHK_PgtB; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 344..396
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 570..783
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 784 AA; 89794 MW; CD6E5AAC6CA06555 CRC64;
MKLIKSNTIA YKLILSFASS PLLIVIISLM ALSTWNNLEK HVSTILEQSV PTLNSSYELE
GSNAKLQSMI IKIQNVSTKI DNNDLSIQLN TQLHMINAIL TDIPDATQLN NAYKTLSKDI
NFLSKQLLQR IDMKRESNKI ENKIRWIQDD INDELQPLRE ELQWQLTLAN KSDHRNDNLE
RINQEFSAIQ KLINNTHELQ RQVTDLKLIQ HPYQVINAFH VLNYKINEIE VANRSLLHHS
STIAYHQLFD QLSKLIRPNA LYQRVLNDRL NLDLNIQKSH LSLLKQLNIL HLLIKKRVHS
AEKTLKNVQT DTQTLISSSS QYLIFCFALS LCISIFVSLY FVNHRIVKRL NDLSANLDAI
NNGRIDFPNN VRGHDEIGLL SLRLQRFCQQ MHEMERTNAL NLINNTPASI ITCDLKGTIE
SVNPSAKRLF HHLDEDDAAL HWQQFSYQNQ DALQIQFKEG SQLHHTGEVS VVLSLFNEEQ
HQHINLELQR FKQGHQTKII ITITDISEHV ETEKLLERHV AQKTLHLSET NQRLLYEIEE
HKKTESDLKN TQTELIQAAK MSVVGQAMTS MAHELNQPLN AMSSYLFSIP LAVSQQRYDE
VDNAVGKIEK LTLRMNKIIN NLRHFSKKHP ADIALKKTDI NAVIEQTFSI LNSKAKQENI
SLKNQIKQPL FTYADNVQLE QVLINIMVNA FDAVAKCTKK DITLSLLSTQ SKLYIIAIED
SGHGFDGRII EHLFTPFTTT KEVGLGLGLS ISQSIIKRFN GSILLASNLQ RGAMLILELP
HYDK
//
