ID A0A080LY13_9PROT Unreviewed; 611 AA.
AC A0A080LY13;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Methyl-accepting chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AW09_000917 {ECO:0000313|EMBL:KFB73812.1};
OS Candidatus Accumulibacter phosphatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB73812.1, ECO:0000313|Proteomes:UP000020077};
RN [1] {ECO:0000313|EMBL:KFB73812.1, ECO:0000313|Proteomes:UP000020077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KFB73812.1}.
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; JDVG02000157; KFB73812.1; -; Genomic_DNA.
DR Proteomes; UP000020077; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 2.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..395
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 400..565
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 611 AA; 65999 MW; 577A82FC2C0FBBED CRC64;
MKTLFAPAIA LLNRVGYTKK FAIMGVLALL AIAMLLLNLY QSLHRVIDSS QRELAGIEVI
KPIARMVQHL QIHRGLSAGM LSGNEAMKDK RAAREKEVSA AFKAVEASLV SELATSAAWK
KVIEAWAAIE KGGLHLVQRE NFEAHNRLIE EVLAFQAVVA DEYALTNDPD IDSTYLIDTA
FEKSPQAIER MGQLRALGTG VLTKKQPLEL SQQVELTVLL AGMNSSVVSL RRNLEKTARY
NPDLHASLQA SITDMSVAAQ KVSALVNQDI LSGTYATLPD DYFALTTASL EKGYQEMFET
LFPTLEKLLQ RRIERAQREL SMSIAVSVLI LLLYAYVSVG LYYATIGSID RLAEDARTIA
TGDLNVRVDL ATRDELKLVG DSLNEMVSAF RGLIENVHHG ASEVLGATKK LAGSAAQING
SSEQQSTAAS NMASAIEQMR SGIEQLSTNA QDANRIASRA GELSADGSRV VGNVVREIER
IAEVVNQSAA IVAELGGRSE RISAIVNVIK EIADQTNLLA LNAAIEAARA GESGRXEIGG
NARQVVEKVA DISHALREQS VASTEIARNV EQVARMAEEN CAAVAGNAAT AAQLERLSES
LEAEVLRFRL S
//
