ID Q893H6_CLOTE Unreviewed; 577 AA.
AC Q893H6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE SubName: Full=Two-component sensor kinase yesM {ECO:0000313|EMBL:AAO36366.1};
DE EC=2.7.3.- {ECO:0000313|EMBL:AAO36366.1};
GN Name=yesM {ECO:0000313|EMBL:AAO36366.1};
GN OrderedLocusNames=CTC_01848 {ECO:0000313|EMBL:AAO36366.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36366.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO36366.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AE015927; AAO36366.1; -; Genomic_DNA.
DR AlphaFoldDB; Q893H6; -.
DR STRING; 212717.CTC_01848; -.
DR KEGG; ctc:CTC_01848; -.
DR HOGENOM; CLU_020473_6_0_9; -.
DR BRENDA; 2.7.13.3; 1526.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd12914; PDC1_DGC_like; 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; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAO36366.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAO36366.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..356
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
SQ SEQUENCE 577 AA; 66452 MW; FDD7FA73F3E00463 CRC64;
MTMRCKTMSL RFKIIITFML CIVLTFSPLL YIMQTKVKDF NMKQLEHETI QLIDSKSNEI
GAWLNHRIGE IKIIHEYPAC KEMNFSQLKP YLTQLNHVFG NQYGTFALGG LDGKGWIDDT
LVIDVSQREY FKKAMSTNVE YVISKPLVSR SDNKPIFLIC YPILNDNKDK IGFINGSVNL
DKISNIIHDI DIHNGFAWIM NKNTDIYSTT KENLNSNYIS LEELSCIANQ SKNKSSGTVA
LKNVHNKDST VFFSSVPYTE NWILCIIVEN KKIHTQINQI INLILFVGLI LLLAAILLSI
VISGSIVKPI HRLKSNMLEI SKGNFDSYYE IKNNDEISIL GQVFNQMLTD IKRLINKVYQ
VEKQKRSAEL RVLQSQINPH FLYNTLDTIQ WKALEYNAFE VVDMINYLSN FFRISLSDGK
EFITISDEVA HVSNYLEIQK IRYKDKISYS MDVDSSLDQY LIPKLIVQPL VENSIYHGLK
LQKHKGIINV SISSKDGFLF IKVIDNGLGM DVEQLRTLRK NLWESIETNH YGLYNINERL
KLAFGKKYSI EIKSELKIGT QVLLRIPLIS EGFECLE
//
