ID A4Y362_SHEPC Unreviewed; 670 AA.
AC A4Y362;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Precursor;
GN OrderedLocusNames=Sputcn32_0665 {ECO:0000313|EMBL:ABP74395.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP74395.1};
RN [1] {ECO:0000313|EMBL:ABP74395.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP74395.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella putrefaciens CN-32.";
RL Submitted (APR-2007) 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; CP000681; ABP74395.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y362; -.
DR STRING; 319224.Sputcn32_0665; -.
DR KEGG; spc:Sputcn32_0665; -.
DR eggNOG; COG3221; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_011260_2_0_6; -.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
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 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 Pfam; PF12974; Phosphonate-bd; 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; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABP74395.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ABP74395.1}.
FT DOMAIN 437..664
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 670 AA; 74683 MW; B1D4A6B2A01772E9 CRC64;
MLFRMMKTVF RFAVSVKWPL SILSTPHSVA IPRKRPRNAV LFLCLLASVK VFAAEPLNQS
AHSGLTDPEV VAQVAIEEPS YQVVDVGVLA IRGYKATINR WQPLMGWLET QIPNSYFRLH
PLTLDELAKG VETQGLDFVI TNPGQSVLLA RQYSLTWLAT LRSPLNNGAA MQVGSALVVR
ADSPYHTLSD LKGRRLGIVS KNAFGGYLTL VYEAQLKGID LPRFVGEIIP LGFPLDNLIY
QLDDKKTSTE RHQPLDAAVV PVCQLEQMQT EGLINIAHYR VLDNQAPAGF NCQVSTHLYP
NWSMAKTNRA SQSLAKSVTQ ALLALPEDHL AAKSADSAGW TTAVSQLAID QLLKDLDMHP
LQAPWWQRAW QWIKLHQQWA WLVLGILVLL NAYHFWLEYR FSRRGRELIN TQRQLNENRA
LLEHAQRIAI AGELGASLSH ELNQPLAAIG HYCHGAEVRL QRGTSPEELQ SVLTLIQQEV
TRADSIISRL RNLLKKRPVS KQPLYLHELV NETVPLLAYE FEQHQINLAV NVNGEPYLQS
LDEVGMQQLL LNLLKNAFDA CVQRLELESS GTEQIITQKP YTPTIDIDLR YQECTLLLTV
TDNGTGLTEE TSLLMQAFYS TKSEGLGLGL VICRDIAESH GGTFSLESAM GGGCQAQVAI
PRKPEPNGAQ
//
