ID A0A0V7ZBT0_9CYAN Unreviewed; 1634 AA.
AC A0A0V7ZBT0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BC008_07855 {ECO:0000313|EMBL:KST61947.1};
OS Mastigocoleus testarum BC008.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Mastigocoleus.
OX NCBI_TaxID=371196 {ECO:0000313|EMBL:KST61947.1, ECO:0000313|Proteomes:UP000053372};
RN [1] {ECO:0000313|EMBL:KST61947.1, ECO:0000313|Proteomes:UP000053372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC008 {ECO:0000313|EMBL:KST61947.1,
RC ECO:0000313|Proteomes:UP000053372};
RA Guida B.S., Garcia-Pichel F.;
RT "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT Mastigocoleus testarum strain BC008.";
RL Genome Announc. 0:0-0(2015).
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:KST61947.1}.
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DR EMBL; LMTZ01000167; KST61947.1; -; Genomic_DNA.
DR RefSeq; WP_058184859.1; NZ_LMTZ01000167.1.
DR OrthoDB; 9799157at2; -.
DR Proteomes; UP000053372; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 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; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000053372}.
FT DOMAIN 24..208
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 229..487
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 812..863
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 878..948
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 952..1004
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1012..1084
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1087..1139
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1164..1395
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1421..1538
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 669..752
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 30
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1470
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1634 AA; 186245 MW; DF8699753996C5A5 CRC64;
MSDFESKNQQ TNLMDSQQAR DFFVVGIGAS AGGLRPLEEF FEHTPTDSGA AFVVVQHLSP
DFKSLMKELL GRKTHMEIYR VEDGMKLQPN SIYLIPPGQN LVVKNRSLQL YKQNRQTQKP
NFPIDLFFKS LATDCGEKAI AVVLSGTGSD GSHGLRLIHE AGGLSIVQDP KTAQFDGMLV
SAIDTAVVDY ILPPVEISKL IYQCLTSCNT IQGGFSNLDA DTGSDSFKIQ QIINVLAHHE
QIDFSHYKSS TLSRRINRRC LILGCENFDD YINRLKILPQ ERDFLRNDLL ISVTAFFRDT
PAWEHLETKI IPSLLREAKP GEELRFWVTA CATGQEAYSL AILLDEAINR SGKNVRIKIF
ATDLDRIALE KATNGIYPET IANDISPERL KNYFTYKDQS FQVSRKLREM LIFAPHDLTK
DAGFTRMHLV SCRNVLIYMQ PKLQQQVLRN LHFSLVPNGI LFLGEAETVS EYEEEFIPLD
KKWKIFQKRR DIRLPLPIRG IEKISRNLIT QSNNSPKSRS SKEQMLEIAF SSFLQEHRTT
CLLVNKDNQV IHFFQDLLSV LKLPLGNPTM EVTRLVPLAL QLPLNTALHR AKREKRAVFF
GGIDLRNEND NENKISINLK VSYHKGNKIA GDFISVTISE SDPVHSQLIT DKSLTGDSFE
LDRAAHARIM ELEYELQETR ENLQATIEEL ETTNEEQQAT NEELIASNEE LQSTNEELHS
VNEELHTVNT EYQSKIQELV ELNNDVNNLL RSTNFGVVFL DRELQIRKFT AAATTAINFK
EGDVGRSLED ITHNTNCFDL RELILQVIET ELPIEKEIKQ VKNDTHLLMR INPYRQEDGD
IDGVVITFVD VDELKTVQEQ VFRVNEALRE SEHSLRKSEE RFRAIFEQAA VGIALLDTDG
KWLKVNQKVC EITGYSEEKL SELKFQDITY TDDIEADLEQ IKQLLAGEIS SYFLEKRYVR
QDDTLVWVNI APSIVRETAD SPGYFIVVIE DISDRKQAEA KLQNASQALT EITERYELAV
RGSKDGIWDW NVETGESYIS PRWKEILGYK DDELANSADT FFSYLHPEDR KQAEEAIKQH
FELHVPFDIE CRMRNKQNEY VWIRNRGQAT WDQSGKPVRM SGSISDITPL KRVEEDLRNV
NHQLALAKES AEAANHAKSE FLAKMTHELR TPLNSILGFT QILYRQSNLQ DQQRKYLDTV
LRCGNHLLNL INDILDISKI EAGAIELNTT EFDLYNIIDS LEQMLQIKSK SKGLQLNVEF
SEDIPQYIRT DEARLRQVLI NLLGNAIKFT DTGNILLQII RGTITESSHS HLNDGINSCY
LTFRIKDTGK GIAERDLSNI FDAFVQAGNN QEYCDGTGLG LAISKNYIDL MGGEMQIQSN
LGKGTTVEFD IPVTIIPKEE FVEHLPKGRI IGLDPEQPKS LILIAEDNSD NHQLLLEIIS
GVGFETIQAH NGQEAVEKWQ KYKPDLVLMD MQMPVMNGYE ATREIRSTSE GKDTTIIIAQ
TSNAFNEDKK LIMSLGCDDF ISKPFQEQIL LEKIAHHLGV KYIYSNDEPQ DLEQRKNPQV
QITPESLAFM SDQWRFQLHQ VASTCNKKDI LKVLADIPED NNSNIQVKQY LINLANKFLF
DVIVDLTTPL EESN
//
