ID A0A2N5Y6C2_9GAMM Unreviewed; 823 AA.
AC A0A2N5Y6C2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:PLW83950.1};
GN ORFNames=CWI75_00920 {ECO:0000313|EMBL:PLW83950.1};
OS Kineobactrum sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Kineobactrum.
OX NCBI_TaxID=1905677 {ECO:0000313|EMBL:PLW83950.1, ECO:0000313|Proteomes:UP000234845};
RN [1] {ECO:0000313|Proteomes:UP000234845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F02 {ECO:0000313|Proteomes:UP000234845};
RA Du Z.-J., Chang Y.-Q.;
RT "The draft genome sequence of Chromatocurvus sp. F02.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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:PLW83950.1}.
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DR EMBL; PKLZ01000001; PLW83950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5Y6C2; -.
DR OrthoDB; 9765776at2; -.
DR Proteomes; UP000234845; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd12131; HGbI-like; 1.
DR CDD; cd11386; MCP_signal; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.490.10; Globins; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00042; Globin; 1.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13188; PAS_8; 2.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF46458; Globin-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS01033; GLOBIN; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000234845};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}.
FT DOMAIN 37..147
FT /note="Globin family profile"
FT /evidence="ECO:0000259|PROSITE:PS01033"
FT DOMAIN 481..517
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 513..575
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT DOMAIN 522..751
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 530..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 722..749
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 823 AA; 89979 MW; 7072E13299833971 CRC64;
MNIDVKLGAF DSDGPLAPHI LEESFGLLAQ NGDRLVARFY EKLFADYPSV KPLFANTSPA
EQQKKLLAAL KLVINNLHSP EQLNQALHQL GERHQGYGAE PAHYDAVSST LLSVMAETAG
DDWNTIYEQA WRSALTVISD VMLSAYQSKR EQTMTSIEHS NQAMKATADS AADINGLRSA
MDGTRMRSAI DNAMTPMMMV DRDLIITYVN HSTVELMKTN EKEMREIYRG FNADKLVGSC
IDQFHANPEH QRRILDNPAN LPFRTDIQVG SLRFHLNITA MLDGDGNYIG NTLEWSDVTE
KRKKEVEVTR LQTAINGSTA NLMMCDNDLR IVYANPAVMK MFRDRANELR QRFPGFDPEN
LIGQNIDQFH RDPSHQRSLL KDPSRLPAQA QINVVGLEFE VNATFIADAE GKYMGNMVEW
KDVTEMIQIR DLVKAAAEGD FSGRLDTSDF KFFNEIGDLL NTLVAVSEQG LTDVGRVVQC
VAEGDLTQTI TEDYQGLFGQ LKNDVNSTVH KLREMIEQIR EGAMSIGSSA SEISQGNTDL
SQRTEEQAAS LEETASSMEQ MTSAVKSSAD NARQANQLSA TAREQAEKGG GVVGEAVAAM
AEISKSSGKI SEIIGVIDEI AFQTNLLALN AAVEAARAGE QGRGFAVVAA EVRNLAQRSA
QAAKEIKTLI KDSGSKVDDG TRLVDDSGKT LEEIVVAVKK VSDIIAEIAA AAQEQSSGIE
QVNKAIAQLD EVTQQNAALV EEAASASKSM DDQSRTLEDL VSIFNIGDED NQPAPVARPR
ARQPEPAAAG RRPPTRAPAR AQAPAPRRPA SSNDSASEDW EEF
//
