ID A0A0S6VPN8_9BACT Unreviewed; 1121 AA.
AC A0A0S6VPN8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=U14_00247 {ECO:0000313|EMBL:GAK49029.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK49029.1};
RN [1] {ECO:0000313|EMBL:GAK49029.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(2015).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; DF820455; GAK49029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S6VPN8; -.
DR STRING; 1499966.U14_00247; -.
DR HOGENOM; CLU_000445_114_15_0; -.
DR Proteomes; UP000030700; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GAK49029.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW Transferase {ECO:0000313|EMBL:GAK49029.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..369
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 370..441
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 440..495
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 566..617
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 635..861
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 886..1008
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 208..252
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 601..628
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 935
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1121 AA; 127032 MW; CCC588CCA9C51A15 CRC64;
MKSERKRIIG LIVIMAITTV FMTGVTIRIL YRIAFNEQRE RLVEICHFSG RLIEAMARFN
RQYTAENLRA IVLQQVLDAQ QHYRLQDRAL EIALGYRDGE MIQYVFRLRQ GDHLEYPPAI
PWSSHLSQAM HLALSGKSGT NISLNAVGKV VLAAYEPVPE LDLGIVAKLE IAHFRAPYIA
ASIAIGLLTT VFVAIGAFLF VRISEPIIRR LSERTSDLEQ FNAQLQQEIT ERKRAEATLQ
ESEERFRQLA ENIHEVFWMT DPKTEEVLYV SPAYEQVWGR SCASLYAHPI SFQASILSGD
LQYSDITLVQ TARGESVNVQ YRIVRPDGEI RWIWSRGFPI RDEQGEVYRI AGISEDITER
KQAEEALRRR EHDFSTLIEH TPDMIVRFDT HLRHVYCNPA VEKQLGITLS VILGKTPSEI
GGSPEQVAFI ESTLRHVLEN KQEMDVEQAY PTPFGLKHFL TRIVPEYDET GHTISLLAIT
RDITDRKLAE EALRDSEEKF RAFVQNAPAR IAAVDQNGIL LFINYTIPER PLEEVIGTSV
YQYLPADVHE QTRQALAVVF DTGDIAKYEM KVVRPDGTSV WYANQIAPLR QGERITAALY
IATDITALKD AQERLQQAKE MADSANHAKS EFLAHINHEL RTPLNGILGY TQILQRDQNF
PSAYLPQITM IHRSGEHLLD LINEMLDLAK IEAGRVELFK EEFHLGHTLT TLVEMVRVRA
QQKDLQFLDE CAADLPSMIV GDARRLRQVL LNLLGNAVKF TEQGRVTLRV VRVPFDAPDN
EMTLTKLRFS VKDTGIGIPE EKRQEIFQPF RQAGNSTYQN QGTGLGLTIS ARLVKLMGGE
IQVESLPEGG SHFWFEAVFP EIRAAQPESS QQTPRILGLP EGTHYRILIV DDHQENRKML
SAMLAPLGFT LIEAANGVEA LHAYETSRPD AIFMDMAMPE MDGVEATQRI RRHEQTTIQN
AAQLTPIPII AVSADVYDQH RGLEAGCQNF LAKPVRFDAL CACLQTHLHI AWCYDAEECR
LSPSVSTERP LIFPPSASLQ QLYEAALIGD VMEVRAQLKA LEQSDSRYET FTKRLREWLA
LFQFQQIRAC LEKAMADAAN GRMNSVPHGE GEKMSEFPEN M
//
