ID R5UV23_9BACE Unreviewed; 763 AA.
AC R5UV23;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BN535_02286 {ECO:0000313|EMBL:CCZ72572.1};
OS Bacteroides caccae CAG:21.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1263037 {ECO:0000313|EMBL:CCZ72572.1, ECO:0000313|Proteomes:UP000017990};
RN [1] {ECO:0000313|EMBL:CCZ72572.1, 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:CCZ72572.1}.
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DR EMBL; CBAN010000056; CCZ72572.1; -; Genomic_DNA.
DR AlphaFoldDB; R5UV23; -.
DR Proteomes; UP000017990; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT domain; 1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..493
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 523..640
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 670..763
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 249..279
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 572
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 709
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 763 AA; 85635 MW; 1FA3415E45A7B9CD CRC64;
MASYRSTKLK VTIGYTLLLA ILLFSLVFVH REMETLSAAD DQENLRTDSL LTLLHEKDRN
TIQMLRVLSE ANDSLLSASE IEEIISEQDS VITQQRVQHR VITKRDSLLT TPKKKGFFKR
LAEVFVPTKQ DSAVLVNTSM EVATDTILEP TTSKDSLQQK IRMATEEKRL QRRKTIRRTS
TKYQRMNSQL TARMDSLIKQ YEEEMTLRAR QDAEMQQEVR MRSARTIGGI AIGAVLLSVF
FLILIVRDIS RSNRYRRQLE EANKRAEDLL IAREKLMLAI THDFKAPLGS IMGYTELLSR
LTEDERQRFY LDNMKSSSEH LLKLVSDLLD FHRLDLNKAE VNRVTFNPSQ LFEEIHVSFE
PLTAAKGLTL QCHVAQELNG RYISDPLRLR QIVNNLLSNA VKFTPKGEIA LTAKYDSSKL
TIAISDTGKG MATEDRERIF QEFTRLSGAQ GEEGFGLGLS IVKKLVVLLE GTIDVQSKLG
EGSCFTVILP LYPVGKSVSE RALEEKTISA EDPVTLPPMK VIRVLLIDDD KIQLSLTAAM
LKQHGIDAVC CEQLEELIEQ LRTSVFDVLL TDIQMPAING FDLVKLLRAS NIPQAKTIPV
IAVTARSEMD IDALQEHGFA GCLHKPFTVK ELLLTVNEGQ LAADEAHITE DMQTVSSLNF
SALTAFSEDD ADAAHSIIQT FIEETGKNAD RMQQALAGKE VDGIAAMAHK LLPLFTLIGA
MEAVPLLNWL ETQRGQCFSE EIGEKTACVL LEIQKVLEEA RKV
//
