ID C0N5T0_9GAMM Unreviewed; 1410 AA.
AC C0N5T0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=NMT1/THI5 like family {ECO:0000313|EMBL:EEF79930.1};
GN ORFNames=MDMS009_1481 {ECO:0000313|EMBL:EEF79930.1};
OS Methylophaga thiooxydans DMS010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=637616 {ECO:0000313|EMBL:EEF79930.1, ECO:0000313|Proteomes:UP000004679};
RN [1] {ECO:0000313|EMBL:EEF79930.1, ECO:0000313|Proteomes:UP000004679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DMS010 {ECO:0000313|EMBL:EEF79930.1,
RC ECO:0000313|Proteomes:UP000004679};
RX PubMed=21478352; DOI=10.1128/JB.00388-11;
RA Boden R., Ferriera S., Johnson J., Kelly D.P., Murrell J.C., Schafer H.;
RT "Draft genome sequence of the chemolithoheterotrophic, halophilic
RT methylotroph Methylophaga thiooxydans DMS010.";
RL J. Bacteriol. 193:3154-3155(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG657897; EEF79930.1; -; Genomic_DNA.
DR RefSeq; WP_008291024.1; NZ_GG657897.1.
DR HOGENOM; CLU_000445_86_2_6; -.
DR OrthoDB; 9813913at2; -.
DR Proteomes; UP000004679; Unassembled WGS sequence.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR InterPro; IPR015168; SsuA/THI5.
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; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF09084; NMT1; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000004679};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002901001"
FT DOMAIN 601..643
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 682..732
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 735..775
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 802..854
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 886..1019
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 1028..1283
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 1410 AA; 160204 MW; CF7FC1B44214A5F1 CRC64;
MPRFSLLLFI LLMPCFALAN QQQMGQHALE PVTLQLKWQH QFQFAGYIAA KEKGFYHDAG
LDVTIHQRTP DIEVIDEVVK GNAQYGIGGM GILSHYANGA PIKALAAIFQ HDALVFLSKA
DSGIVSPYEI AGKRVMFDSS TGNDAVLRVL LDDAGMSYND ITIVPQDFAI ESLSNGQVDV
MSAYITSQPF EFRQKGEAIN IINPQNYGFD FYGDLLFTSV EELKNHPGRA ERMLQASLKG
WDYALQHPEE IIQIIKNKYN SAISVEQLRY EARETNKLIV PEVIPLGTIQ PARLRRIADL
YAKLGVVPRL SDKTLNHFIH RQQKTTLSPQ VQQWLTEHPV LKVGIDPDFA PYEWINEKGE
YVGLAAEYIR LLEQRLDVSF QIVHDKPWHE IMDMAKRGEL DMLSCLNQTD SREEHLDFTA
PYVSNPVVIV NADRNGYVGS LDNLNGKTVA IEEGYFTHET LRSDYPEITL LLTENTQQAL
EKVAAGEADA YIGDAAYANY AVKKNDLLNL QFAGQISETS AYRIGISKAN PELLEAINMV
LDNLTEAERK VIEDKWLGLT VTSGPQLATL IKISSAVMVL FLLFAYWIYR LRKSGRALAQ
SETRLREVLN ASPVPQGILN EVGQVTYLNQ AFITTFGYTL ADIPTVNDWW QKAFPEKTHR
ETIQAEWQLH IEDSLNRSDT LKPVESDVVC KNGDKKTVIC NATHVASATD KHTLVILYDI
SERKKAEERL KMSGRVFNQA HEGILITDAK GLLVDVNPAF SEITGYSREE VIGKNPSILQ
SDKHSRVFFQ EMWTSLEEKG HWQGEIWNLK KNGQLFAELL TISTLVDERG ETLHYLGLFS
DITQSKEQQH ALELMAHYDM LTQLPNRTLF ADRFHQAIAH SKRNHSLLAV VFLDLDGFKP
VNDRYGHDVG DQLLIEVAQR IKASIRQDDT ASRLGGDEFV LLLNDISSVD HCERLINRIR
HAIELPYQLD EDTISLSASL GITIYPLDDA DADTLLRHAD QAMYQAKLAG RQRHHIFDAL
HDQQISQQQN QYKAIQDALK ADQLVLHYQP KVNMGTGQII GVEALIRWNH PEHGLVLPGR
FLPAIQGTEL EIHVGNWVIE HVMQQVEAWL RDGIEMEISI NISSHHLQWK GFFEQLDHVL
GRHPHVPANL LQLEILESSV LSDINKISSI INTCRNVLGI RISLDDFGTG YSSLTHLRHL
PVDVVKIDQS FVRDIIDDPN DYTIIDGVIG LTQAFHHQVI AEGVETIEHG LMLMTMGCEL
AQGYVIAKPM PAKDFTEWFS NYKPNPQWLK HAEASLDSQQ TMIQLMRIQG HHWLDKIIHN
LQSTPDKIEH WPLMNHKKSH FMHWLEQAKK QNLFNKTWRE DIKLAYTELY HEANSLKYQF
QEGYEDAGEI GIKGLYERFQ TIESLLREFD
//