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Database: UniProt
Entry: A0A1R4L598_9SPHI
LinkDB: A0A1R4L598_9SPHI
Original site: A0A1R4L598_9SPHI 
ID   A0A1R4L598_9SPHI        Unreviewed;      1198 AA.
AC   A0A1R4L598;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
DE   RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00924638};
DE            EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00924638};
GN   ORFNames=FM120_32230 {ECO:0000313|EMBL:SJN51745.1};
OS   Sphingobacterium faecium PCAi_F2.5.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1255690 {ECO:0000313|EMBL:SJN51745.1, ECO:0000313|Proteomes:UP000188305};
RN   [1] {ECO:0000313|EMBL:SJN51745.1, ECO:0000313|Proteomes:UP000188305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCAi_F2.5 {ECO:0000313|EMBL:SJN51745.1,
RC   ECO:0000313|Proteomes:UP000188305};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
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DR   EMBL; FUKX01000055; SJN51745.1; -; Genomic_DNA.
DR   Proteomes; UP000188305; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 3.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF05227; CHASE3; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 3.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS01002602};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000188305};
KW   Kinase {ECO:0000256|SAAS:SAAS00924871, ECO:0000313|EMBL:SJN51745.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01002785};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188305};
KW   Transferase {ECO:0000256|SAAS:SAAS00924820};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
FT   TRANSMEM    177    199       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      220    272       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      532    754       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      810    923       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      932   1048       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN     1078   1195       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   COILED      428    508       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     859    859       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   MOD_RES     981    981       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   MOD_RES    1128   1128       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   1198 AA;  134726 MW;  72FF7C4212C1DF06 CRC64;
     MPKPFLRNLQ IGFGFSLLLL LASSTASYIS IKEQISNRTK VDHSRRVIAS ANKILNDLQN
     AETGQRGFLL SGKETFLEPY LISLQTLPKS LDRTQQLVSD NLLQSQVADS LTYLVKSRLG
     ILTNLIEVKR EGKQVTLAQL EEGKHYMDSC RNIIARFISV EEGFLDKRSN ELNKSSLYTS
     IFVVIAAIVS LLITVVFYLR IREDFIKREG LQKSLREKDE EISRRLKATQ RIANQIASGD
     YSVHVNDEEE DDLGSLGGSL NQMANALQKS FDDLNNNEWR QTGLAQLNEI LVGNKTEDIL
     VADALHQLIR YGNVTNGAFY LLEQDRIVLK DAYGLENRMV KSFNIGEGMI GQVFKEGKVK
     RFANLQDKDY VVSFANGQVQ INYILLLPVF VDFTCIGVIE LGSIDAFENV KLPFFIDATR
     NIGIAISAAK SRDQVQQLLE ETQTQTEELQ AQHAELENLN TELEAQTHKL QSSEEELRVQ
     QEELVQSNQE LEERSKSLEE KNYLIAERNL EIQHKAEELA LSTKYKSEFL ANMSHELRTP
     LNSILLLSRL MSEDTDGNLN EDQIESAKVI QSSGTSLLNL IDEILDLSKI ESGKMELDYQ
     DVKLDEVIHD LQNLFLPIVK DKSLAFNIKT ESGIPDMIET DRLRLDQILR NLLSNAIKFT
     HEGSITLTIS EDKEHGDQLL FEVKDTGIGI AEEKQKIIFE AFQQADGSTR RKFGGTGLGL
     SISREIARLL GGKISLKSKE GEGSVFTLIL PKRKISETIK PTSEELIDII ASDINEMTTI
     VSESVASNIV YNIPEEVDDD RDNIVKGDKV ILIVEDDTAF AKALLKYTRQ QQYKGIVVVR
     GDIAADIAAR YLPLAILLDI QLPIKDGWEV MDEIKSNPQT RHIPVHIMSS LRVKKESLLK
     GAIDFINKPV AIEQIGLMFK KIEDALTRYP RKVLIVEENP KHASALSYFL SNFNIAAEIK
     TNVDDSVQAL SSDSVNCVIL DMGVPDKIGY ETLEAIKNNE GLENLPIIIF TGKNLSHAEE
     VKIKQYADSI VIKTAHSYQR ILDEVGLFLH LVEENTTDQQ KRKANKLGSL SEVLTGKKVL
     IADDDVRNIF SLSKALEKYQ MNVISATNGK EALLQLDNHP DVSIVLMDMM MPEMDGYETI
     RLIRKHPQYT KLPIMAVTAK AMTGDREKCI VAGASDYISK PVDTDQLLSL LRVWLYEN
//
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