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Database: UniProt
Entry: C3L4M4_AMOA5
LinkDB: C3L4M4_AMOA5
Original site: C3L4M4_AMOA5 
ID   C3L4M4_AMOA5            Unreviewed;      2279 AA.
AC   C3L4M4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Aasi_1629 {ECO:0000313|EMBL:ACP20942.1};
OS   Amoebophilus asiaticus (strain 5a2).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC   Candidatus Amoebophilus.
OX   NCBI_TaxID=452471 {ECO:0000313|EMBL:ACP20942.1, ECO:0000313|Proteomes:UP000001227};
RN   [1] {ECO:0000313|EMBL:ACP20942.1, ECO:0000313|Proteomes:UP000001227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5a2 {ECO:0000313|EMBL:ACP20942.1,
RC   ECO:0000313|Proteomes:UP000001227};
RX   PubMed=20023027; DOI=10.1128/JB.01379-09;
RA   Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA   Rattei T., Horn M.;
RT   "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT   reveals common mechanisms for host cell interaction among amoeba-associated
RT   bacteria.";
RL   J. Bacteriol. 192:1045-1057(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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; CP001102; ACP20942.1; -; Genomic_DNA.
DR   STRING; 452471.Aasi_1629; -.
DR   KEGG; aas:Aasi_1629; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   HOGENOM; CLU_000445_34_2_10; -.
DR   Proteomes; UP000001227; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:UniProt.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001227};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          234..493
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1719..1791
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1794..1847
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1876..2113
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          2139..2270
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          1838..1866
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         2200
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2279 AA;  257124 MW;  76C87E6B02FE8562 CRC64;
     MQSCVNLTNS PIPIKKGQTD HTQEIIPQIA IRSIVDIEFT TKGGHLITFY EKTGRLQAEV
     IEQNEGLSKV HMLPVYIEEG MDIAQVAQLN EAAQKRFIHI NLPKRKDSGS IWIGHAGLKG
     GSNTGKNKGK EKLKDDQYQA LEEKKLIAQA GQLISSKQEI NHLKAKGEGN SPSEFNKTYD
     LSVPVEKELH ATSSIKEEQK QLIHANLAKS EQTGYLQVGG MELKRENHLV LPGYKLLHCL
     HEGTSSNIYR AVRLSDECPV VIKVSTQKVL TEKKAQRFRR EFELGQQVHS PYVVRYLELK
     QDAAYGMAIV MEDDQAVELN AILPPTGFSN QEFLEIAIQI VEGLQAIHAA NIIHSDLKLN
     NILIQPTTNL IKIIDFNRSS TLRQERPPTM PMMVGTLTYI SPEQTGRVNR SVDYRTDFYS
     LGVTFYRLLC GEPPFTAKDA LGLIHQHLAR QPIPAHQHKP TVALSLSRMV MKLLEKEAEN
     RYQSCEGILH DLIVCLSAFK ETGAIPEFEL GQQDFSSKLT LSQNLYGREK EIKTLEKAFE
     RVSEGRCEAL MVAGEPGVGK TMLIQEIQKP IALQHGYFIT GKFDQLNKNV AYSAFAQAFN
     SLVQQWLTED QTSIMQWKIR LMESLGTQAS LLIKVIPSLA LLIDEQPETA IADMSQAKNV
     LNWIFQEFIK FCTTPSHPLV IFLDDLQWAD QASLELMTYL MTQPSIKHLL WIGAYRDTEV
     TPSHPALQSI TALQEASITV QTLTLAPLQL KNLCQWITDS LHKSIMDAQP LVELIFQKTA
     GNPFFVKLFL QSLYDEQLLT FAPQSHWQWD LDKIRQHPAT ENVITLMTYQ IQQLPVSTQQ
     ALSIASCIGH RLVLSTLQTA MACSHQELEK SLQPALNSGI LIQTDHEIYF AHDRVQEAAY
     HLLPETIKTR THLMIGRRLL VSPTSEEKLL SDIVAQFNRC CSLVTDSQER LHIARLNLKS
     GQKAKQSTAY GVALDYLHTI PKWIDTEILW QSDYPLAFTF HKELAEVEYL GGYMDTSQAI
     IADMQPRLQS NLDKVDIYHL LIIQKTLQGH YQEAIALGHK TLQLLGIWLP LDNLTEFIQK
     ATDDIKQKLH NIPLSSLLNA PLVVEPEKKA LLKILESLVA ACYFAGSELL TAATLMSIDL
     ALTYGHAPES CLGYTVYGSL LCNRFEEHAL GYEFGQLSIQ LAKKLQAPAQ HCKSLLIMLA
     LISPWSKSIQ QLPALLTDGY KVGLACGELE YAGHCVSMKA QLLFYQGMSL AKVQQEILPL
     LQFTYNTKNQ VAINTIQTVQ RLVVNLIGNT LDEWNFDADA ITEARFKKSC QQASSFYSLC
     LYQILKAQTF YLYGHFKQAF GQLALVKQHL VLILSQYATA LFNWYDSLVR LALYPTSSIA
     DQQIYLQQVI KNQQQMQKWQ ASCPANFAHK YALVEAEIFK LQENYQQAEA YYDQAIELAD
     RHGFIQEKAL AAELAAKYWL TRGKTLSAQG YLNTAFNGYK QWGAKRKLMQ FKTQYEYLLK
     DLVPPSLSYL TVNQETTLSS NTLRYLDLSS ILKASQTISS EIELPKLLRN MMQIIIENAG
     AQQGAVLFVE AGDTVVVQAE YASDNTITTL QKIPLADWEH GAHTVIQYVK RLHQSVVLDN
     ATIHEQFKID PYINRTQAKS ILCIPLLKQT ELRAILYLEN NLMTHAFTPE HMQTVLILTA
     QIAISLENAR YVAEQLALTQ QLAEQSTRRK IAEESLHVVT HDLKLALEAS QAGTWSWWID
     SNKVVWDATM YALFGLTPDT FRGTFEEVRE RVHPEDKEQF EKNIDNCVKQ STPHSIDYRV
     IWPDGSQHMI TAHGQVYRDT TSGSPIKMTG VCLDITERKK LEQDRLEALQ QAKEKEQQRA
     DEAERYFKQQ EEFINTVCHE IRNPMNGISN TVVFLEEKIT SLKKLKESLP GSFQPELKEL
     LPTLEEDIQT IQHCVNHQLV VINGVLNLSR LEAGKEKLLL KPFKPKTIIE ESILLFTSQL
     KTKQLNLIID LPKQAIAIQG DPERFKMILI NLISNAIKFT EKGHIKISFQ TQAVDSTHVE
     LVIRVEDTGI GMTPEEQSCL FQRFSRPLSS QYEGSGLGLA ISKKLLDLMG GTIQVDSVKG
     QGSTFTIHLT CEMVDIGEKL IYQKPPAPLP ILPPIAVKHI LIVEDNIVNQ KILRRQLEAA
     GYTCMVADNG QKAIEAIGAI EEVETLEQWN LAAFDLILMD LEMPVMGGIE ATGWIRKKEQ
     QLGVPSIPII GLSAYAEEIY GETAKKAGMD AYNTKPYRKE ELLKTIQSLL SRPLEPASE
//
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