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Database: UniProt
Entry: A0A434AXH6_9BACT
LinkDB: A0A434AXH6_9BACT
Original site: A0A434AXH6_9BACT 
ID   A0A434AXH6_9BACT        Unreviewed;       693 AA.
AC   A0A434AXH6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DLK05_05290 {ECO:0000313|EMBL:RUT79232.1};
OS   Ancylomarina longa.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Ancylomarina.
OX   NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT79232.1, ECO:0000313|Proteomes:UP000282985};
RN   [1] {ECO:0000313|EMBL:RUT79232.1, ECO:0000313|Proteomes:UP000282985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT79232.1,
RC   ECO:0000313|Proteomes:UP000282985};
RA   Fu T.;
RT   "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT   southern Okinawa.";
RL   Submitted (NOV-2018) 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:RUT79232.1}.
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DR   EMBL; RJJX01000004; RUT79232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A434AXH6; -.
DR   OrthoDB; 1116352at2; -.
DR   Proteomes; UP000282985; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282985};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..693
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019275394"
FT   REPEAT          159..192
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          239..272
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          279..312
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          456..674
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   693 AA;  79905 MW;  72FFFE49A35F0D31 CRC64;
     MNMRLLVLFL LVFQLSASER SMAEISPKND NQEYEVNRDQ LQTIYELGTS YLQVSLDSAN
     VYANRLRCKS VFIGDTLYLG YANLLEAKVS YRKSEYNRTV NFIEEALKQL SDSLLVDRAN
     CFNICGNAYI KMGNYKLALK SHLTCLKIRN QLGDEYFISK SLNNIGSVFF KLRDYNSAID
     YYNKSLEIRI KQKDLTGIAL LNNNIGNIYF EKGDRVNALI KYFNAFHTID KEQNIYWKPL
     LLKNIGEVYQ SKGEISKAIV FYQRALYEAR EMDDQAAVAT SWIHLGRAYL NEKRYNQSLG
     AIKKALSISK KYKIPELELE GDRCLSLFYE QRGDYQNSLR FQKEYSLLKD SLFRQNNRKE
     IAEMSAKYKL DKIEKENIYF KQKSKIQELE IEKQNTRNKY FSILSVLVLA VVIYTVRSTK
     QKKRHNVLLK EKNKTIYKQN KELGQLNATK DKFLSIVAHD LKNPFNAVLG FSDLLIDRYF
     DIEESTRMEY LEIIHKSAAN GSVLLETLLT WSRSKMGIMT YNPIEFDLID VASDELEILK
     DKALIKNIEL EFKFNMSYCV KADIDMVRTV IRNLGNNAIK FTKEYGKVIL SVSERSGLLY
     FSVRDNGIGI KFDDLSKLFK LDSNFTRPGT SNEKGTGLGL ILCREFIEKN GGSIGVQSQE
     GVGSEFWFTL KINSSEILKK TSTRGAEVKS LSC
//
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