ID I4B1Y6_TURPD Unreviewed; 565 AA.
AC I4B1Y6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Turpa_0641 {ECO:0000313|EMBL:AFM11293.1};
OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS (Leptospira parva).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Turneriella.
OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM11293.1, ECO:0000313|Proteomes:UP000006048};
RN [1] {ECO:0000313|EMBL:AFM11293.1, ECO:0000313|Proteomes:UP000006048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC {ECO:0000313|Proteomes:UP000006048};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL Submitted (JUN-2012) 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; CP002959; AFM11293.1; -; Genomic_DNA.
DR RefSeq; WP_014801811.1; NC_018020.1.
DR AlphaFoldDB; I4B1Y6; -.
DR STRING; 869212.Turpa_0641; -.
DR KEGG; tpx:Turpa_0641; -.
DR HOGENOM; CLU_482266_0_0_12; -.
DR OrthoDB; 310468at2; -.
DR Proteomes; UP000006048; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006048};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT COILED 42..69
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 266..304
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 565 AA; 63981 MW; 6DB5E9B64BE67852 CRC64;
MLNSFYRIRN FYRNLKIRYK FFLTMAVVLM IAVPALSYVF ISQSEQLLIK SLEERIELLN
SNFSILTRNS LQENSFSFLQ GMVRDAALRQ KEVRALVIVN ARGTIIATNN ENDYPLFGDL
RSMHPGDLFR GGKNVLRRLK REGVIESMHL IHAAAPTEVA EKTESREIVA TLYVVVTTDF
LENSVRNLWL YSLLLTLVFT TLAFFTAYRA GLHLARPITR LAQDVQQIAS GNLAVKIEPG
NKDEIGQLIS DVERMQASIL RMLFEVNEGK EKIQEYADHL EDMVKEQTAE LRETLEQVQA
LKNQQDADYY LTTLLVEPLR VNLANNKNVN VQFVVRQKKR FPFRQWTVEI GGDICIAHSI
ELRGSQFTVF MNGDAMGKSI QGAGGALVLG AVFQSIIERT RMTENVKSLP PAEWIKATFL
ELSKVFLSFD GATYASLVLG AVDEETGDMF HINADHPRIV HYRGGQAEFI DSEFRLRRLG
FQIPEDTVVV RQTRLLPGDI VIAGSDGRDD IILGSVENNT EINEDEGLFL RHVTATQGNL
NEILNRIVDS GQLTDDLSLL RIHFH
//
