ID M3HTU1_LEPBO Unreviewed; 470 AA.
AC M3HTU1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=PAS domain S-box protein {ECO:0000313|EMBL:EMG00995.1};
GN ORFNames=LEP1GSC123_3650 {ECO:0000313|EMBL:EMG00995.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMG00995.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMG00995.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMG00995.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG00995.1}.
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; AKWO02000037; EMG00995.1; -; Genomic_DNA.
DR AlphaFoldDB; M3HTU1; -.
DR BioCyc; LBOR1193007:G11KN-2918-MONOMER; -.
DR Proteomes; UP000011783; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000011783}.
FT DOMAIN 22..77
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 81..131
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 214..266
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 277..470
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 115..142
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 470 AA; 54143 MW; 13E5F924AA681952 CRC64;
MESILITEKH YQLLFDFSQD GLVIHSEGKI LKANDALIRM LGYDSIEEVI GRPILQFIHH
RSQNIVKQRI QKMIQEGVGV GIVEEEFIRK DGSTLFVEVA STTFFESDRQ YFQAIVRDIN
SKKRAELELE RLRSKLKVTQ ERLCGVIEGT KDAICAVDIN FRVIAFNSSF ELNFWKLYGK
KIEEGNLLPE LIWDPLERSV VIENWSRALR GEVYTTERMM HGLVQDVAIF EISYSSIRDS
SHNLIGATQI IRDITERKND EEKLKKTLEE KEVMLKEIHH RVKNNLQVVA SLLGLQAEYS
QNEKISLILK ECERRIQSMA LIHKELYQSE NITKIDFCDY LNTLLISLLH SFGKEKKVEF
DISSKPNFVS IETAIPLGLI VNELVTNSLK YAFLNEREGR ISVKLRLDMG ESVLEIGDNG
IGMPEKFDLD KSESLGLRLV EILSKQLRGK FVLLPTGEER GTKFQIRFKT
//
