ID A0A1R1I6Y0_9RHOO Unreviewed; 1502 AA.
AC A0A1R1I6Y0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE RecName: Full=PAS domain S-box protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BJN45_04485 {ECO:0000313|EMBL:OMG54495.1};
OS Azonexus hydrophilus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Rhodocyclales; Azonexaceae; Azonexus.
OX NCBI_TaxID=418702 {ECO:0000313|EMBL:OMG54495.1, ECO:0000313|Proteomes:UP000187526};
RN [1] {ECO:0000313|EMBL:OMG54495.1, ECO:0000313|Proteomes:UP000187526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS02 {ECO:0000313|EMBL:OMG54495.1,
RC ECO:0000313|Proteomes:UP000187526};
RA Salah Z., Rout S.P., Humphreys P.N.;
RT "Alkaliphiles isolated from bioreactors.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine +
CC H(+); Xref=Rhea:RHEA:24902, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58754, ChEBI:CHEBI:58805; EC=3.1.4.52;
CC Evidence={ECO:0000256|ARBA:ARBA00051114};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24903;
CC Evidence={ECO:0000256|ARBA:ARBA00051114};
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:OMG54495.1}.
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DR EMBL; MTHD01000002; OMG54495.1; -; Genomic_DNA.
DR RefSeq; WP_076092581.1; NZ_MTHD01000002.1.
DR STRING; 418702.BJN45_04485; -.
DR Proteomes; UP000187526; 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: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 CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR FunFam; 3.20.20.450:FF:000001; Cyclic di-GMP phosphodiesterase yahA; 1.
DR FunFam; 3.30.70.270:FF:000001; Diguanylate cyclase domain protein; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL 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; IPR052155; Biofilm_reg_signaling.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR44757:SF2; BIOFILM ARCHITECTURE MAINTENANCE PROTEIN MBAA; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 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; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000187526}.
FT DOMAIN 2..184
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 195..468
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 829..875
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 951..997
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1024..1076
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1108..1240
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 1249..1502
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
FT COILED 622..702
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 14
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 41
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1502 AA; 167204 MW; 637389E959933762 CRC64;
MPPLRPYLVG IGASAGGLEA LSALIAALPT NLGISYVVLQ HLSPTHRSMM VQLLGRETAM
AVQEVEHGGQ PEPDTIYVAP ASRNVIIKDG CFVLIEGPRE AMPRPSVNVF FTSLAAEKIE
DAIGVVLSGT GSDGAAGLRD IKAAGGYTFA QDPQSAKYAG MPQSAIDTGC VDWVLTPDGI
AEEIAIIARS HGTVTVTTKP PVAATALKKL LMKVKQQTRI DFSGYKEGTL WRRIERRMAA
KHVVSLNDYL TLVDASPEEL EHLGKDILIS VTAFFRDPES FEALREMLRS ILQAKQPGDE
IRVWVPGCAT GEEAYTIAII IAETLGPSVT QYRIQIFATD IDLNALAIAR KGSYADSALA
DLEPGLVVRY FQKVGNRLEV ARHIRDMVVV ARQDIIQDPP FLRLDVVSCR NLLIYLQNDP
QAKVLATFHY GLNPGGILFL GQSEGIFQQE SLYDVVDKSA RIYRRRDGES RMTMPSFRLP
ENVERTAPAV APDAERRLLD AAVRRYVPAS VLINSNFDIL QIHGDVSQYL TVLPGKPNFN
LQHLLRREMR ADLQLLQHQA EHKQESVFGR RHSIKTLDGQ RDIRLAVHAL ERGVVSPFFL
VSFEILPPLE TVDANGAATS AVAEDGRNVR ELEDELVSTR ERLQTVIEEL ETSNEEMQAL
NEEVVAANEE LQSSNEELEA ANEELQSTNE ELTTVNEELQ VRTGELADTL NDLENIQNSV
GFPILVCNED LGLSRFNSPA AALFSLSSAS IKQPMTMLRL PPGMQDFSGL VRQAIESNRP
VEGPVFSSER HYLLHVSPYE TKMRGGRGAI LVMLDHTERL VAERELTKNR EMLLAIMNNS
TSIITLKDLA GRYEFVNRQF ETFFDVNAEK VIGKTDAKVL SRKVADDFRA KELDVVRQRK
ALEFEDHLSF PSVGDRFLHS IRFPLLTEDG TVYSICTQSV DVTEHKHAED QLRLAARVFD
RAGEGIVVTD AKQIILTVNE AFTQVTGFSG EEVIGKTPAV LASGKHDKEF YLEMWSRLQN
QGWWQGEVWN RRKNGEIYPE WLTINSVKDS EGKVVNFVGI FSDITIVKES QRRVEFLATH
DELTSLPNRA LFLDRVRQAV ARTTRTDSTF AVLFIDLDNF KVVNDSMGHA AGDDLLIEIA
RRMRECVRGS DTVARFGGDE FAMLLEDASA EDAEMTARRV AEAMERPHLI GRQSVYPSAS
IGICLFPNDG LDAETLLKNA DSAMYQAKDS GRSTHHFFTD ELKQAADERL KIETGLRGAI
ERNELFLMYQ PQIDIATGRL VGVEALLRWQ HPEDGLIPPM KFIPMAEKSG MIDQVGEWVA
ATACRQMALW IAQGHQVPRV SINVSADQLR RTNLPALMRR LLGHYRLDAT RIVIELTETA
LLDNVERVQQ MLRELKTLGI QLSIDDFGTG YSSLAYLRRF ALDELKIDKS FVADIAQNLD
DRAIAQTIMA MSQTLGFSVV AEGVESEEQL AVLREIGCNI GQGYLFARPM MPDDLVKGFN
AR
//
