(data stored in SCRATCH zone)
SWISSPROT: Q3Z4M2_SHISS
ID Q3Z4M2_SHISS Unreviewed; 482 AA.
AC Q3Z4M2;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 08-MAY-2019, entry version 104.
DE RecName: Full=Sensor protein {ECO:0000256|RuleBase:RU364088};
DE EC=2.7.13.3 {ECO:0000256|RuleBase:RU364088};
GN Name=ybcZ {ECO:0000313|EMBL:AAZ87290.1};
GN OrderedLocusNames=SSON_0521 {ECO:0000313|EMBL:AAZ87290.1};
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87290.1, ECO:0000313|Proteomes:UP000002529};
RN [1] {ECO:0000313|EMBL:AAZ87290.1, ECO:0000313|Proteomes:UP000002529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87290.1,
RC ECO:0000313|Proteomes:UP000002529};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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;
CC Evidence={ECO:0000256|RuleBase:RU364088,
CC ECO:0000256|SAAS:SAAS01126420};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|RuleBase:RU364088}.
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DR EMBL; CP000038; AAZ87290.1; -; Genomic_DNA.
DR EnsemblBacteria; AAZ87290; AAZ87290; SSON_0521.
DR KEGG; ssn:SSON_0521; -.
DR HOGENOM; HOG000126763; -.
DR KO; K07644; -.
DR OMA; ITETAQF; -.
DR BioCyc; SSON300269:G1GL2-611-MONOMER; -.
DR Proteomes; UP000002529; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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_c; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR01386; cztS_silS_copS; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
DR PRODOM; Q3Z4M2.
DR SWISS-2DPAGE; Q3Z4M2.
KW ATP-binding {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS00925949};
KW Cell inner membrane {ECO:0000256|RuleBase:RU364088};
KW Cell membrane {ECO:0000256|RuleBase:RU364088};
KW Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW Kinase {ECO:0000256|RuleBase:RU364088, ECO:0000256|SAAS:SAAS01003914};
KW Membrane {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS00925724};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS00925310};
KW Transferase {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS01003669};
KW Transmembrane {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS00926038};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS00926160};
KW Two-component regulatory system {ECO:0000256|RuleBase:RU364088,
KW ECO:0000256|SAAS:SAAS00924981}.
FT TRANSMEM 12 36 Helical. {ECO:0000256|RuleBase:RU364088}.
FT TRANSMEM 187 206 Helical. {ECO:0000256|RuleBase:RU364088}.
FT DOMAIN 207 260 HAMP. {ECO:0000259|PROSITE:PS50885}.
FT DOMAIN 268 482 Histidine kinase. {ECO:0000259|PROSITE:
FT PS50109}.
SQ SEQUENCE 482 AA; 54234 MW; CF5D22A8F0B17557 CRC64;
MVSKPFQRPF SLATRLTFFI SLATIAAFFA FAWIMIHSVK VHFAEQDIND LKEISATLER
VLNHPDETQA RRLMTLEDIV SGYSNVLISL ADSHGKTVYH SPGAPDIREF TRDAIPDKDA
QGGEVYLLSG PTIMMPGHGH GHMEHSNWRM INLPVGPLVD GKPIYTLYIA LSIDFHLHYI
NDLMNKLIMT ASVISILIVF IVLLAVHKGH APIRSVSRQI QNITSKDLDV RLDPQTEPIE
LEQLVLSFNH MIERIEDVFT RQSNFSADIA HEIRTPITNL ITQTEIALSQ SRSQKELEDV
LYSNLEELTR MAKMVSDMLF LAQADNNQLI PEKKMLNLAD EVGKVFDFFE ALAEDRGVEL
RFVGDKCQVA GDPLMLRRAL SNLLSNALRY TPTRETIVVR CQTVDHQVQV TVENPGTPIA
PEHLPRLFDR FYRVDPSRQR KGEGSGIGLA IVKSIVVAHK GTVAVTSDAR GTRFVIMLPE
RE
//
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