ID D0TSZ4_9BACE Unreviewed; 1353 AA.
AC D0TSZ4;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0102_02282 {ECO:0000313|EMBL:EEZ03220.1};
OS Bacteroides sp. 2_1_22.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469588 {ECO:0000313|EMBL:EEZ03220.1, ECO:0000313|Proteomes:UP000005775};
RN [1] {ECO:0000313|EMBL:EEZ03220.1, ECO:0000313|Proteomes:UP000005775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_22 {ECO:0000313|EMBL:EEZ03220.1,
RC ECO:0000313|Proteomes:UP000005775};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA McDonald J., Allen-Vercoe E., Strauss J., Ambrose C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 2_1_22.";
RL Submitted (JUL-2009) 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; GG705175; EEZ03220.1; -; Genomic_DNA.
DR RefSeq; WP_008770826.1; NZ_GG705175.1.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000005775; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 5.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EEZ03220.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EEZ03220.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1353
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003016425"
FT TRANSMEM 788..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 842..1054
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1104..1219
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1251..1350
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1152
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1353 AA; 155316 MW; 9F74CFEBB2FE92FA CRC64;
MNSLKKTTIC LLFLCIGVNC VFSEVPEQIN FSYISINEGL SQSTVFSIDQ DQRGNMWFAT
YDGVNKYDGY SFTVYQHNEE DPNSIANDIS RIVKTDSQGR VWIGTRDGLS YYDEEKDKFR
NFFYEKKGKR QQINGIAEIS PEQLLISTQE GLTMFDIKES KFVDDSFSTA MHKLIASALY
RQGDIIYIGT PVDGLYSYSI PQKKLEKITP ITETKQIQAI LQQSPTRIWV ATEGTGLLLL
NPKTKEVKAY HHSSSNPKSI SSNYIRSLAL DSQNRLWIGT FNDLNIYHEG SDSFVSYSSN
PVENGSLSQR SVRSIFMDSQ GGMWLGTYFG GLNYYHPIRN RFKNIQRIPY KNSLSDNVVS
CITEDKDKNL WIGTNDGGLN LYNTKTQQFT HYILQENERE IGIGSNNIKA VYVDEQKSLV
YIGTHAGGLT VLHRNSGKME SFNQLNSQLV DENVYAILPD KGGNLLLGTL SALVSFNPEK
KSFTTIDKEK DGTPFTSQRI TILFRDSHKR LWIGGEEGIS VFQQEGLEIE KVPILPESSV
TKTFTNCIYE ADNGIIWVGT REGFYCFNEK EKKIKRYTTA NGLPNNVVYG VLEDTFGRLW
VSTNRGISCF NPETERFRNF TESDGLQSNQ FNTSSFCRTS SGQMYFGGIN GITTFRPELL
LDNPYTPPVV ITKLQLFNKT VRPDDETGIL TKNINETESI TLKSWQTAFT IEFVVSNYIS
GQHNTFAYKL EGYDKEWYYL TDKRTVSYSN LPQGTYHFLV KAANSDGKWN TVPTMLEIIV
LPIWYKTWWA IMIFLATFIG FITFVFRFFW MRKSMEAELE LERRDKEHQE EINQMKMRFF
INISHELRTP LTLILAPLQE IINKISDRWT RNQLEYIQRN ANRLLHLVNQ LMDYRRAELG
VFELKVKKEN AHQLIQDNFL FYDKLARHKK ITYTLHSELE EKEELFDPNY LELIVNNLLS
NAFKYTESGQ SITVTLKEEN NWLVLQVSDT GIGIPINKQG KIFERFYQIE SEHVGSGIGL
SLVQRLVELH HGRIELDSEE GKGSTFSVYL PQDINIYKPS ELASNDAKNE EDQVYSTNSK
EMYFIDTEKV KNEAIETGDK KRGTILIVED NNEIRHYLSS GLSELFNTLD AGNGEEALEK
LKENEVDIIV TDVMMPVMDG IKLCKNVKQN IRTCHIPVII LSAKSETKDQ MEGLQMGADD
YIPKPFSLAI LTTKIQNMMR TRRRMLERYS KSLEVEPEKI TFNAMDEALL KRAVAIVEKN
MDNIEFSTDE FAREMNMSRS NLHLKLKAIT GESTIDFIRK IRFNEAAKLL KDGRYTIAEV
STMVGFNTPS YFATSFKKYF GCLPTEYIKK AKG
//
