ID A0A927IG59_9BACT Unreviewed; 1074 AA.
AC A0A927IG59;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE SubName: Full=PAS domain-containing protein {ECO:0000313|EMBL:MBD5780837.1};
GN ORFNames=IEN85_15155 {ECO:0000313|EMBL:MBD5780837.1};
OS Pelagicoccus enzymogenes.
OC Bacteria; Pseudomonadati; Verrucomicrobiota; Opitutia; Puniceicoccales;
OC Pelagicoccaceae; Pelagicoccus.
OX NCBI_TaxID=2773457 {ECO:0000313|EMBL:MBD5780837.1, ECO:0000313|Proteomes:UP000622317};
RN [1] {ECO:0000313|EMBL:MBD5780837.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NFK12 {ECO:0000313|EMBL:MBD5780837.1};
RA Feng X.;
RT "Pelagicoccus enzymogenes sp. nov. with an EPS production, isolated from
RT marine sediment.";
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
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:MBD5780837.1}.
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DR EMBL; JACYFG010000038; MBD5780837.1; -; Genomic_DNA.
DR RefSeq; WP_191617945.1; NZ_JACYFG010000038.1.
DR Proteomes; UP000622317; 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 CDD; cd16434; CheB-CheR_fusion; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 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; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF27; PROTEIN-GLUTAMATE O-METHYLTRANSFERASE; 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; PF13596; PAS_10; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 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; 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); 1.
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.
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:UP000622317}.
FT DOMAIN 1..189
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 222..468
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 858..1071
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 650..708
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1074 AA; 120508 MW; 588A31A47975DFF0 CRC64;
MKPEYIVGIG ASAGGLEALV QFFSEMPSRT GLSFVVVQHL SPDFKSVMDE LLSRHTDMPI
HLVEDKVEVE ADSVYLIPPK KEMEMSDRCL YLKDKETRGS LSLPIDVFFT SMAKDIGAKG
IAIVLSGTGS DGSRGIVDVH DAGGLVIAQD EESAKFNGMP RSATDTGLVD FVLSPTEMPK
VLLEHIGGSV SDPGIVAAPG PKTQMDQYLA IFQRLRSAFK TDFSYYKATT VNRRIERRMQ
HHKVDTLEQY VAVMDRKPQE VHLLYQDLLI GVTKFFRDLD AFALLEDKVI PSIVRGKSSG
EQVRIWVPAC ATGEEAYSIA ILFQEAIERF NLKLDVKIFA TDLHAESVTF AAAGIYSPES
LELISKSRLE RHFKVHGEAY QVNADLRKMI VFAEQNLLKD PPFTKMDFVS CRNLLIYFQP
LAQKKVISMF LFSLNVGGTL FLGPSETLGD LEGEFDSISR TWNMYVKRKD VRIAPLINLP
EQVDIAARSG ERNRQNSSLF GVSRQRREDV ELLHVYDALL GEYMPPSLLV GPKNELIQIF
GDASNYIRTP RGRTSLDVLN MIEGSLRLAV STALKRVENK RVAFTLNNVP LDENAEERVL
LDITVKPLRD EQYLLVQFLE RRGAETTPDD VSEMSFDADA ESLSRIFDLE KELQYTRENL
QATIEELETT NEELQATNEE MLASNEELQS TNEELQSVNE ELFTVNTEYE KKNHELILLN
TDIDNLLQST EIGTVFIDSE RRIRKFTPAI ASVFNLLPMD IGRPFEHITF NLVDSENISQ
LVDRVIESRE PIIREARDRS GNWHLMRIYP YMTGREQSAG AVLTLVDISA IKETEAALKS
RTDALSNAKL DLEQFAYAVS HDMQTPLRAV SGYLDLLKKR LEGEDQELQE YLEFAHSGAF
KLKEMINGLL TYTRIETRAA DFEEFSLESA LNEVLATKTV ALEEKGAEVV SESCNLIVYG
ERRFVVYLLS ELIDNALCFV GAGPPRIVVK AEAQDGQTLV SVRDNGRGIE PVNQDTVFKI
FYQEKPEQHP EGLGVGLAVC RRIALKHKGT ISLDSTPGIG TCVSFTLPSR PEDV
//
