ID A0A285JXK3_9ENTR Unreviewed; 470 AA.
AC A0A285JXK3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN ORFNames=SAMN02744775_01221 {ECO:0000313|EMBL:SNY65045.1};
OS Enterobacter sp. CC120223-11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY65045.1, ECO:0000313|Proteomes:UP000219512};
RN [1] {ECO:0000313|EMBL:SNY65045.1, ECO:0000313|Proteomes:UP000219512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY65045.1,
RC ECO:0000313|Proteomes:UP000219512};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Member of a two-component regulatory system.
CC {ECO:0000256|RuleBase:RU364088}.
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 ECO:0000256|RuleBase:RU364088};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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DR EMBL; OBEF01000004; SNY65045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285JXK3; -.
DR Proteomes; UP000219512; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
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 InterPro; IPR048590; CusS-like_sensor.
DR InterPro; IPR006290; CztS_silS_copS.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR01386; cztS_silS_copS; 1.
DR PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF21085; CusS; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|RuleBase:RU364088};
KW Cell inner membrane {ECO:0000256|RuleBase:RU364088};
KW Cell membrane {ECO:0000256|RuleBase:RU364088};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364088};
KW Membrane {ECO:0000256|RuleBase:RU364088};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364088};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364088};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU364088};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU364088};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012,
KW ECO:0000256|RuleBase:RU364088}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364088"
FT DOMAIN 198..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 259..470
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 470 AA; 53501 MW; 9A988E68B9FF96DC CRC64;
MCWKKDKMLI PRNLSITLRL TLYFSVAMTL VLYSVSGLLY STMRNQLSQK DENELRSTLQ
FQQEIATTIS ERQGPTDLWQ QELFEFIARQ DRLSLRIISP DGKVWAQSKN MRVPNADFPA
PSRDFSYRSW RYHRGDISEK YLIASTNFIL KGNEPWLVQA ALNVSRNNEI IEDYWQRMQI
AVALAIVVFS SIGYWLARRG LLPLRKISRE IEYIHAEDLD TRLATQHWPS ELSALASSFD
RMMTRLEASF KQLSRFSSDI AHELRGPINN LISAASVTQS KDRSPQEYRD ALAAIVEEGE
RLSRMISSML FLARADNSRE MLHREPLNSE TEFERLMDYY DILAEEKNIC LTREGDVSFH
GDAIHVQRAL SNLLSNAIRH TGPGGTVHLK ASLEDNVVLL AVQDNGEGIS PEHLPFIFDR
FYRVDDARSS AGNTGLGLAL VKTIAELHGG RVRVESTLGQ GSCFTLILPL
//
