ID   F3ZSU1_9BACE            Unreviewed;      1457 AA.
AC   F3ZSU1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Bcop_2007 {ECO:0000313|EMBL:EGJ72182.1};
OS   Bacteroides coprosuis DSM 18011.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ72182.1, ECO:0000313|Proteomes:UP000018439};
RN   [1] {ECO:0000313|EMBL:EGJ72182.1, ECO:0000313|Proteomes:UP000018439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ72182.1,
RC   ECO:0000313|Proteomes:UP000018439};
RX   PubMed=21677860; DOI=10.4056/sigs.1784330;
RA   Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA   Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT   strain (PC139).";
RL   Stand. Genomic Sci. 4:233-243(2011).
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; CM001167; EGJ72182.1; -; Genomic_DNA.
DR   RefSeq; WP_006745338.1; NZ_CM001167.1.
DR   STRING; 679937.Bcop_2007; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_007691_0_0_10; -.
DR   Proteomes; UP000018439; 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   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   InterPro; IPR033405; DUF5112.
DR   InterPro; IPR033406; DUF5113.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF17139; DUF5112; 1.
DR   Pfam; PF17140; DUF5113; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EGJ72182.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018439};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:EGJ72182.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        421..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1012..1031
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          292..325
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          617..847
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1457 AA;  169534 MW;  1F2AC24C0B72CB61 CRC64;
     MGIAPTKEVR YIDGLNSKAS KYGYTSLDSV SIYAQRAYKE AKHYELGKAE ACNHLGFYHF
     MRMNFDESAH FYQEVGKHTI NELELLISDI GMMKIFQRTA QSKLFYDYRN SALARMKRID
     EDRTVFDKIK EKKRLNYAYS EFYIVSAIYF YYLQQEELAA EAIADLDQRK EDALNWNAIS
     TDTIQLLYYK YIKGATGLVK GKTATEKLLA SFDELFQTWR LARAQGIIYF EANAAQGMAN
     ILARPVNYEL IYHERIHLLG GLGYPIDSIL PLRLGESALK LFKTYEDIYQ IAGAHVTLAQ
     YYNYRGEYNK ALEVLKSALD YVNQHHRLYY KDHHDSPDDL KLYEEDVNQN PIEIQWIEDD
     VLTVPEWIAR IREQLSVAYA GVGNKAASDY NRNVYLDILD LVRQDKELES RYASLQKEER
     FINSLLSLLF FLVIVLGVLF YLVNKHSRKK TTLYLQRLEN SLTVCRDLTA SLPLKASRLE
     DVVEPIVQII RRFLEKELGV ERIYLRIKAI DEEELMYDTA PDKEKDTGLY SSSFDLKTRD
     SSLENGMFRV FTAKKLGKED LSFIAILSPY MVWAIENGLH FMDLGEEREL LEKKLFITNQ
     HNIQDKRENI LKRANMRIVY GIQPYLDRIR NEVRKISYAT YTKEKEVRQL KYQYIDELLD
     TIQEYNEVLA LWIKIKQGEL SLQIANFELG ELFELLEKGV RSFEQKKISL HIKPTDVVVK
     ADRALTLFML NTLLENARKF TSEGGEVKVS ANASEEYVEI AVSDTGVGMS DEDIQKILYE
     KVYDSSEIGG DNPDVKEQKG SGFGLMNCKA IIEKYRKTNP VFHVCNFDIQ SEKGVGSRFS
     FRLPYGVKKT FMLILILLGG GFSTSAQEFS FQMVPDSIRL KLLYEASDFA DAAYFSNVDQ
     TFSQTLQYVQ LAIDKLNQFY LQNSFSKEPL MKMAGDDTPA EVEWWNRKFE TSYHVILDIR
     NEASVAYLAL KDIDSYNYNN KAYTMLYKLT SKDDSLDRFC KLLERSTSNK QVALIIVVTL
     IISFLLVYYV VYVRRQLSRR WSLEQVLDIN ERIFSASLHY TVNGDEKKTE ADLTTIPRQI
     IEKSFAEFNE LLAVDAMGII LQDEEKQQLS TTLYPMEEQL DAETIHRCIQ ERIWISLENE
     VYIPLETTLG AKSEVVGVFY LRRRDRSELA EEKLFLELIV RYMSTVLYNT MIRTAGRFRD
     ISLVFDDIHR LDWENNQIHV QNRVLDNCLS AIKHETIYYP SRLKQIVDEL RRTSLTEERE
     MAEVKVMFDL VEYYKGVFTI LSLWAKKELE RATFRRSIFS VNDLMGDMEK LFQRRNKKRA
     IPLTMDIEIE PHLELVGDEK LVEYLLEMLI LDALAMPIAG ALKWKIESEG DFVSFTFTDT
     RKNYSEETLN NLFYPTLERM KATSEEGLPG TTYLIAKEII REHDEFVGRR GCRIRAFACP
     QGGYSLYFTL TRKPQIV
//