ID A0A3N5CVL4_9SPHN Unreviewed; 1491 AA.
AC A0A3N5CVL4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=PAS domain S-box protein {ECO:0000313|EMBL:RPF72827.1};
GN ORFNames=EG799_11495 {ECO:0000313|EMBL:RPF72827.1};
OS Aurantiacibacter spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2488860 {ECO:0000313|EMBL:RPF72827.1, ECO:0000313|Proteomes:UP000275232};
RN [1] {ECO:0000313|EMBL:RPF72827.1, ECO:0000313|Proteomes:UP000275232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E23 {ECO:0000313|EMBL:RPF72827.1,
RC ECO:0000313|Proteomes:UP000275232};
RA Zhuang L., Luo L.;
RT "Erythrobacter spongiae sp. nov., isolated from a marine sponge.";
RL Submitted (NOV-2018) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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:RPF72827.1}.
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DR EMBL; RPFZ01000001; RPF72827.1; -; Genomic_DNA.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000275232; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 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; 2.
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; IPR036804; CheR_N_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF07536; HWE_HK; 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; SM00065; GAF; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 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; PS50113; PAC; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000275232};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..184
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 197..438
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 778..828
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1073..1123
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1342..1453
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1456..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 628..715
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1460..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 7
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT MOD_RES 1392
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1491 AA; 164406 MW; 7C75788CF0094D2E CRC64;
MVAVGASAGG IEALKSFVSQ IPADICASFV ILQHLAPDHE SQLTGILSRA APLPVQEAEQ
DAKVEPGHIY VLTPGEYITL VDTGLFVEHP SEPRGKRMPI DHFMRSLAET AGAQSVGVVL
SGTGSDGTLG LRAIKGAGGV SLTQSPETAL YDGMPRSAID AGAVDEVGDI GQLCATIAEL
ARRMAEPREN AGFNRNDLSG VVSLLKTRTG HDFSAYKAGT LARRVRRRMN LLRFDGLNDY
LQHLRDDGDE LKRLFDDLLI NVTSFFRDRE VWPAVVDQAI KPLARRASED GDPVRIWVPA
CSTGEEAFTL AMLMEEQCAA TSEACNWQIF ATDLDDEAIA HGREGVYAES ISNDVSQERL
SRFFDRENHG WRVKKALRER VVFAQQNILS DPPFSKLDFV SCRNLLIYLE TGVQDELLET
FHFALREGGF LLLGTSETTG AHKREFASVD NKAHLYTRLP GRASARLSAQ GERHRGDGKI
IQMPASRSRR DRRFELAEQV RRSLLQRYAP AAIAVHSDGE IAYFHGPVRR FLDHPEGEPS
TSIYDLLPAP LRSRVREALT KVKSGNRPSH RSAKVRFPDR DTTVCVECEP VRDGDQTLYL
VTFIEQEDKD ERDAGRDAER TGGEGDYATQ LENELAIVRE DLQTTVEELE TSNEELKASN
EEAVAANEEL QSANEELETS REELQSLNEE LITVNNQLEE KIVEVERSKD DLRNLFTSTR
LPVLFLDPDL VINGFTPAMN QLVELREGDI GRRVTDLAFK VADDDLLADV QSTLGDLSPS
ERQVQAEDGG VYVRRVQPYR TADQRIRGVV VTYGDITEQA EAARLLARRE RQQRIIAELS
QTALAARELP HFLDEMCALL RVAMDCDYAK VLELDEDADR LVLAAGAGWK TGLVGSASVE
TGVKSQGGYT LKVEHAVLVT DFDGERRFDP PPLLTDHSVQ SGISCLIEVG GKPWGVLGLH
DRNARKFTEE DLSILKSAAN VAAATIMQIA REAHLARESL LLSLAIKTAE MGAWRYDPEH
ELVVWDEQLR DMMGRGFTRR KPSRDEFFDM IVEDDRQRIR DAFDDTVRQG TPFNAEFRLR
RGDGRTIWMT ARGERLVEDG KTTVLGLNAD ITEAKLAEEQ NRFIMRELDH RVKNVLAIIR
SIAKITGKNA PTFEEFIKGF ERRLHAMART HSLLADARWQ GARLRTLVED ELAHSRSGGN
VVIEGEEVAV SPAAAQALSM AFHELTTNAL KYGALSVPDG TLTVEWSRRT AENGKDMLDL
SWTETGGPDV EAPVSEGFGS TVIERILGAQ LQATAKIDYR RSGLVVTCSF PMERLTTAPK
AAAAPVAAVP PEADLAPIAD ARVLVLDDEW LVAEQHARAL IAAGAHVVGP YHSLEEARTA
LNEEAVDLAM LDFNIDGRAV TELYPDLDRL GIPCLIVSGY GSDLDIEEDA QAREFLAKPA
SPAAMLGRVA GMLRAAGTGD DKETAGDGDE NHDRDDAEAS VNREASPSRS S
//
