ID A0A080MK79_9PROT Unreviewed; 1417 AA.
AC A0A080MK79;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=rpfC_3 {ECO:0000313|EMBL:KFB77714.1};
GN ORFNames=AW06_001088 {ECO:0000313|EMBL:KFB77714.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77714.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77714.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:KFB77714.1}.
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DR EMBL; JDST02000018; KFB77714.1; -; Genomic_DNA.
DR STRING; 1453999.AW06_001088; -.
DR Proteomes; UP000021315; 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; cd00088; HPT; 1.
DR CDD; cd00130; PAS; 4.
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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR036641; HPT_dom_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
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; 4.
DR SMART; SM00091; PAS; 4.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW Transferase {ECO:0000313|EMBL:KFB77714.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..375
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 550..602
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 603..673
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 754..800
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 825..879
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 915..1135
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1162..1278
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1321..1417
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1211
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1360
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1417 AA; 157194 MW; F8915C6395342C58 CRC64;
MKARPLSSFL ARLIWLCIAP LLLLAIWLAW DNLQELEARH LREGANLAQN QAIAHDNFLN
TRIGALRMLA DSPLADDPRR WPDLYAEALG FQKSFGTHVI FAASTQQMRF NTRTPFGTPL
PMLPRPKGRS ATLLALETGQ PQVGDLFFGP VAQVPLVAIV VPRVQDGKVA HLMITTIETA
QLQQRLDKVA LPDGWSLTLV DGTGAHLARR APAGFDAARD VAEDHRFVVA LAKSAWSVVV
EIPRSNHQAE QMKSGGILAA AILLATLFAI LGGTLTSLRI GREVKALAMP PGSAGPPLEI
TEIAATQSQM NALNADRNAS EERFRRLFDL APLPLALVTE DGRILTLNAR FQAVFGYTPE
DLPTVDTWFE RAYPDPVLRK RARSTWQRAA SGEDIPPRAY RVVCKDGLAR DMLISSLPQP
EGSLAVFIDI SVQKQAMQAL EATLAEQGKA RLATLNQIED TNAALRRAES LAAALQESQN
RLQLLIDHAP AALAMFDREM HYLAVSRRWR EDYALGEREM LGHSHYDIFP EIPAAWRKVH
QRGMAGETLA ADEDRFERAD GRVQWLRWEV RPWPTADGSV GGIVIFSEDI TVRKAAAETV
RASEEKLRNI LDFSPDAVFI VAADRRFLYH NRQAAVLLGY SGDEFAELCI DDTIPDELHR
EVLERFRLNL EGQTQFFETQ LRRKDQSLVD VEINGMRLPD GTVIGQVRDI TSRKMAEQAL
RKSMEEQRLA QMAALSLMED AQSERSRAEA ALETVRKLSL AVEQSPESIV ITDLTGAIEY
VNDAFIKVSG YDRTEVIGQN PRLLNSGKTP PGNFAALWRA LKRGDTWKGE FYNRHKDGSE
FIEFAIVTPI RQPDGTITHY VAIKEDITER KQVSIELDTY RNHLEELVAT RTTELVEARL
RADAANQAKS AFLANMSHEI RTPMNAIIGL THLLQRSQVT DEQRERLHKV DTAAYHLLSI
LNDILDLSKI EAGRMQLESM DFALSDILEN TRVLIAEAAK TKNLVVDIDA CHTPRWLHGD
PMRLRQGLLN FASNAVKFTE HGRIVLRAQR VTEDAQGLLL RFEVEDTGIG IPADKLAGLF
QAFTQADVST TRQYGGTGLG LAITKRLAQM MGGDAGAEST PGQGSRFWFT ARLEHGYGVV
PVAGGAQIRN AGANLRSRRG ARILLAEDNA VNREVAIELL RAVDLEVDSA ENGRIAIDKA
RGHDYDLILM DMQMPELDGI EATRAIRSWP GRDRVPILAM TANVFEEDRR ACLFAGMNDF
IAKPIDPDQL YTTLLKWLPA SVRTANAGKS ETRAETADLY SRLARVAGLD IEQGLSITLG
RIEFYARLLS MFVDSHAPDS EGLRMLACSD DQEALGQLVH ALKGTAGNIG ALHLSGKASS
LMTNLREHRP NLYSQVMALA DELEQLINGL RQALRRP
//
