ID A0A1H9K6A9_9PROT Unreviewed; 574 AA.
AC A0A1H9K6A9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SEQ94691.1};
GN ORFNames=SAMN05421690_100429 {ECO:0000313|EMBL:SEQ94691.1};
OS Nitrosomonas sp. Nm51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=133720 {ECO:0000313|EMBL:SEQ94691.1, ECO:0000313|Proteomes:UP000198732};
RN [1] {ECO:0000313|EMBL:SEQ94691.1, ECO:0000313|Proteomes:UP000198732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm51 {ECO:0000313|EMBL:SEQ94691.1,
RC ECO:0000313|Proteomes:UP000198732};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FOGH01000004; SEQ94691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9K6A9; -.
DR STRING; 133720.SAMN05421690_100429; -.
DR OrthoDB; 9813966at2; -.
DR Proteomes; UP000198732; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198732};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..263
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 268..497
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 519..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..506
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 519..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 61490 MW; 2091A1783FCF8493 CRC64;
MVNNMTIKSK LVILIGMLSS LLIAIGGLGL YGIYESNQGL KTVYEDRTVP AVDLGFILDR
MQRSRINMIF AANLNDIEVA KTRTQLIVER DAEIAEIWAK YIVTTLTPEE EQLANTWVRQ
WDAYKEVRDR IMRLSVAGDF AAAVQTRRND AQAKFDAVDE TMFNLISLQG RVAEQEFAQA
QNSFNTILMI ISVAIVTGVI LAIVIGMMLI RSIIGPLNNA VAVAKAVASG DLTSRIEVNS
TNETGRLMQA LKQMNGNLVD LVGKIRSGTD SIFTSSGEIA SGNLDLSQRT EEQASSLEET
AASMEELTST VKQNADNARQ ANQLASGASE VAVKGGAVVG QVVQTMSAIN DSSKKIVDII
SVIDGIAFQT NILALNAAVE AARAGEQGRG FAVVATEVRT LAQRSAAAAK EIKELISNSV
NKVEDGTRLV DEAGTTMDEI VNAVKRVTDI MAEISAASQE QSSGIEQVNQ AVTQMDEVTQ
QNAALVEEAA AAAESMKEQA EELARAIASF TLSDSMLKKS AASSRKPENV TQLPNRATSA
KHVMSSSNES AAAQAVSKPK KVAIGGGNDH WEEF
//
