ID R5UX06_9BACE Unreviewed; 1330 AA.
AC R5UX06;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN535_02965 {ECO:0000313|EMBL:CCZ73272.1};
OS Bacteroides caccae CAG:21.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ73272.1, ECO:0000313|Proteomes:UP000017990};
RN [1] {ECO:0000313|EMBL:CCZ73272.1, ECO:0000313|Proteomes:UP000017990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:21 {ECO:0000313|Proteomes:UP000017990};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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};
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:CCZ73272.1}.
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DR EMBL; CBAN010000099; CCZ73272.1; -; Genomic_DNA.
DR Proteomes; UP000017990; 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; cd00082; HisKA; 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; 3.
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; IPR018062; HTH_AraC-typ_CS.
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; 1.
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; 2.
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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:CCZ73272.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:CCZ73272.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 764..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 806..1023
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1064..1179
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1215..1314
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT REGION 1310..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1112
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1330 AA; 151494 MW; DED12A5E06E629ED CRC64;
MKYIVYIFLL FPILVTAQTY KYIGIENGLS NRRIFNIQKD DQGYMWFLTN EGMDRYNGKD
IKHYKLNKDD NSVASQIHLG WLYATPEAGL WVIGRKGRLF QYEKQYDRFT IGYKLPDISK
TISYGYVDHN NNIWLCCNDS IVLYNIKNAH TFQFPNILHS NITAIEQIDD NHFFIATETG
VRYAKLKNGA LQIIPTETLD YFHTQVSVLY FQQQQKKLYI GSFERGIFVY DMLSQEIIRP
EADLSDVNIT RIRPLNETEL LVATEGMGVY KLDMNKCILE RYISANYQSY NEMNGDNIND
VFVDESKRIW LANYPTGITV IDYRYENYHW MKHSMGNKQS IVNDQVHAVI EDSDGDLWFG
TSNGISLYNS GTGEWHSFLS SFNHQLKDKN HIFITLCEVS PGIIWAGGYT SGIYKINKAD
LSVEYFSPYL LSHINMRPDK YIRDMIKDSK GHIWSGGYYN LKCFDLATNS VRLYPGVSSI
TAIAEKDSHN MWIGTAMGLY LLNRDSGKYE YIKLEAGSTY INTLYQADNG LLYVGTNGAG
VFIYDAQNKK FEHYIAKNSA LVSNSIFTIL PEVDGRIMMS TENGVTSFHT KEKIFHNWTK
GEGLLPAYFN ASSGVLRKNK NFVFGSTDGA IELPQNVKFP DYVYTKMIFS DLNISYQPVY
PGEEDSPLEK SINDTDVLEL KYNQNTFSFR VSTINYDSPG NALYAWKLDG FFEKWTEPGT
ANLIRYTNLP PGKYTLYVRA ISREEHDIVF EERTMRIVVT HPFWSSWWAI TCYVLLVILG
FIFILRVMNL RKQKKISDEK TSFFINTAHD IRTPLTLIKA PLEELLDEEP LSANGITRAN
TALRNVGTLL RLTNNLINFE RADVYSSELC VSEYELNTYM HEVYETFSSY AAIKHIDFTY
ESSFSYLNVW FDKEKMDSIL KNILSNSLKY TPENGKVSVS VSESNDSWKV IIEDTGIGIP
SSEQSKLFKL HFRASNAINS KVTGSGIGLM LVGKLVRLHG GKINVESIEH QGTTVRIVFP
KSNKHFQNAG LIPPAKPLEQ TPELTVPNIS ATPVNTVETT NSQRILIVED NDELRSYLVS
SLSSMYHVQA CGNGREALII AKEFWPDLIL SDIMMPEMRG DELCVAIKND IETSHIPVLL
LTALGDENNI LDGMSIGADA YIVKPFNVRI LKASIANLLA NRALLRSRYA NLDIDSEPMI
PSANGTTSLD WQFISAVKKS IEENMDNTGF SVDVLCELHH MSRTSFYCKL KALTGQSPTD
LIRMTRLKRA TQLLKEGGHT IAEISDMTGF SESKYFREVF KKHYKMSPTK YAKEGSNSSP
IITEDNLSDD
//
