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Database: UniProt
Entry: A0A1M5JMD0_9BACT
LinkDB: A0A1M5JMD0_9BACT
Original site: A0A1M5JMD0_9BACT 
ID   A0A1M5JMD0_9BACT        Unreviewed;      2141 AA.
AC   A0A1M5JMD0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488109_0144 {ECO:0000313|EMBL:SHG41420.1};
OS   Chryseolinea serpens.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Chryseolinea.
OX   NCBI_TaxID=947013 {ECO:0000313|EMBL:SHG41420.1, ECO:0000313|Proteomes:UP000184212};
RN   [1] {ECO:0000313|EMBL:SHG41420.1, ECO:0000313|Proteomes:UP000184212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24574 {ECO:0000313|EMBL:SHG41420.1,
RC   ECO:0000313|Proteomes:UP000184212};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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};
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DR   EMBL; FQWQ01000001; SHG41420.1; -; Genomic_DNA.
DR   STRING; 947013.SAMN04488109_0144; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000184212; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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; 11.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 2.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 7.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
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   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 7.
DR   Pfam; PF18947; HAMP_2; 4.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 12.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 3.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 5.
DR   PROSITE; PS50885; HAMP; 11.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SHG41420.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000184212};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          233..285
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          325..377
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          417..469
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          509..561
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          601..653
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          693..745
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          785..837
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          877..929
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          969..1021
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1061..1113
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1153..1205
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1452..1685
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1755..1868
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1877..1992
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          2022..2139
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1179..1206
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1383..1442
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1804
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1926
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         2072
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2141 AA;  232822 MW;  29AD50BEC06DBF9B CRC64;
     MKTKAALKEK RTPAKKSASN VRVKKNGSNG HDTDSLHADG HAISSDQIGS KELLRVLTEV
     KNGNFSVRMP IDEVGLNGKI YDTLNEIISL NEKMMQEFTR AGNTIGKQGK LTQRIEIPST
     KGAWSEGVNS LNVLISDLVH PTIEIAHVIS SVAKGNLSQE MPEEIGDHRL EGEFLRIAKE
     VNYMVKQLNL FSMEVTRVAR EVGSEGKLGG QAKVKGVGGV WKDLTDSVNH MAGNLTNQVR
     NIAEVTTAIA RGNLSKKITV DVKGEMLELK NTINTMVDQL NSFSSEVTRV ALEVGTEGRL
     GGQATVKGVG GVWKDLTDSV NQMAGNLTAQ VRNIAGVTTA VATGDLSKKI TVDAKGELLE
     LKNTINTMVD QLNSFSSEVT RVAREVGSEG QLGGQADVPG VGGTWKDLTD SVNQMAGNLT
     NQVRNIAGVT TAVANGDLSK KITVDVRGEM LELKNTINTM VDQLNSFGSE VTRVALEVGT
     EGKLGGQATV KGVGGIWKDL TDSVNQMASN LTGQVRNIAG VTTAVANGDL SKKITVDVRG
     EMLELKNTIN TMVDQLNSFG SEVTRVALEV GTEGKLGGQA TVKGVGGVWK DLTDSVNQMA
     GNLTAQVRNV AGVTTAVAKG DLSKKITVDA KGELLELKNT INTMVDQLNS FSSEVTRVAR
     EVGSDGQLGG QANVPGVGGT WKDLTDSVNQ MASNLTNQVR NIAEVTTAVA KGDLSKKIAV
     DVRGEMLELK NTINTMVDQL NSFGSEVTRV AREVGSEGQL GGQADVPGVG GTWKDLTDSV
     NKMADNLTNQ VRNIAEVTTA VAKGDLSKKI TVDVKGEMLE LKDTINTMVD QLNSFASEVT
     RVAREVGSEG KLGGQATVKG VGGVWKGLTD SVNQMAGNLT AQIRNIANVA IAVANGDLSK
     KITVDVRGEI LQLKDTLNTM VDQLRGFASE VTRVAREVGT DGKLGGQAFV PGVAGTWKDL
     TDSVNQMAGN LTDQVRNIAG VTTAVANGDL SKKITVDVRG EMLELKNTIN TMVEQLNSFA
     FEVTRVAREV GTEGKLGGQA EVRGVAGTWK DLTDSVNQMA SNLTGQVRGI AKVVTSVAKG
     NLKQKLSINA LGELAQLTDT INEMIDTLAV FAEQVTTVAR EVGVEGRLGG QASVPGASGT
     WKDLTENVNQ LAANLTTQVR SISEVASAVT KGDLTRTIRV DAKGELEALK DTINQMITNL
     RETTLRNQDQ DWLKSNLAKF TQMLQGQKDL KTVTRRILSE LAQVVSTHYG AFYILQQDED
     MAQVKLKLFA AYAYKEERTI PREFAIGEGL VGQCALEKEK ILLTNVPQGY VKINSGLGRA
     KPANLIILPI VFENNVKAVI ELASLDVFNE THLDFLDQLT ESLGIVLNTI ETNTRTEELL
     AQSQSLAGEL KTQQEELRRT NDELQDKAFL LVKQKDEVEA KNKEVEEARK SLEEKAEQLT
     LTSKYKSEFL ANMSHELRTP LNSLLILAQQ LYENAEGNLN DKQIRYAKTI HSCGDDLIQL
     INDILDLSKI ESGFISANIS SVRIGEIASF VETTFKPISE ARNLKFKIET DYTLPATMDT
     DIQRLNQILK NLLSNAFKFT EKGEVALKIF EAQRTWKPGV ATLDNASTVV AFSISDTGIG
     IPQEKQLIIF EAFQQAEGST SRKYGGTGLG LSISRGLAEL LGGTIELDSE AGRGSTFTLY
     LPLNSLASAA PRQVSESIKV IQELQLDNDG NQINNLLGNL RITNEGVEAR NMDIVNEMIN
     DSGDDRSHIQ ANDKVVLVVE DDLRFGKIVI EKAHEKGLKA VVATNYLEVF DFINRFSPIA
     ITLDVKLPDT SGWKVIDLLR NDLTYRHIPI HVISGEENRV LALKRGARSF LLKPLNNDLL
     NNLFNDIVTY DRKEKKSILI VEDNELDSSQ IAKMHRDDKV DVTIAGTAKE ALELVQAEEF
     DCIILDYTLP DMPGSELLHE VSRAKADLTP VIVYSAKDFS KTEMSNVNLN SSSHIVKGVN
     SIEYLLEETI SHLHINHKSL APEKRRIIEN IRNKEDILTG KNILVVDDDV RNLFALTTVF
     ERFNINVITA ESGREAINIL TENPKIEMVL MDIMMPEMDG YETTQKIRRE HKNNTLPIIA
     VTAKAMKGDR QKCIEAGASD YITKPVKIDQ LLSLMRLWFC K
//
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