ID A4Y9R9_SHEPC Unreviewed; 562 AA.
AC A4Y9R9;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 111.
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_2987 {ECO:0000313|EMBL:ABP76702.1};
OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP76702.1};
RN [1] {ECO:0000313|EMBL:ABP76702.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN-32 {ECO:0000313|EMBL:ABP76702.1};
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};
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DR EMBL; CP000681; ABP76702.1; -; Genomic_DNA.
DR AlphaFoldDB; A4Y9R9; -.
DR STRING; 319224.Sputcn32_2987; -.
DR KEGG; spc:Sputcn32_2987; -.
DR eggNOG; COG5000; Bacteria.
DR HOGENOM; CLU_000445_114_4_6; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF51; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABP76702.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 184..236
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 360..562
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 78..105
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 562 AA; 62802 MW; B30B7A65657DEF27 CRC64;
MLIRTKIIIY SIACCAFGVL LSFALVKYIL SEASVVATPH AIKTPDNNVT FDFAELEKNL
ASIELALNNS EPLQQAAAMQ AHQRAEQIKA ELQKLEQLKQ AQLQIKLFTL EQLKEGAFNS
MPHIVEPLRV EPLSILPPKA PVSSVAPAEI VASEPAASLT LGEGVIVLLL ACCVCGLGIA
WLTRHLGRSL DSLEVGLLNF SDNDFSVSIP EHGEGQLKTL AQLFNHSAAK LRQERQYIYQ
RELLLDKVIQ SSPNVMLLLD DHQRLIYAND AARHLFHKKG RMEGLSLDEL LVDLPEALAL
ALKHEKNGLF AMGEDEMETW YISRGQFLLN NQQHNLILLK QMTRELNRQE VAVWKKVIRI
ISHELNNSVA PIASMVNSGR LLTQDIDDPR LTLIFDTIEN RTNHLSQFIF NYARFAKLPL
PQRCQVSWAQ FTAQLTQHYP FKLKDDLPEI DGYFDQGQME QVLLNLLKNA HESGSNPEDV
TLSIRYQTLV DGAGFSIAIE DRGAGMSGEV LEQALLPFYS TKQSGTGLGL PLCREIIEAH
DGCISMHNRS DGGLLVRLWL PQ
//