ID A0A411PM35_9GAMM Unreviewed; 548 AA.
AC A0A411PM35;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=HAMP domain-containing protein {ECO:0000313|EMBL:QBF84584.1};
GN ORFNames=EXU30_19345 {ECO:0000313|EMBL:QBF84584.1};
OS Shewanella maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=2520507 {ECO:0000313|EMBL:QBF84584.1, ECO:0000313|Proteomes:UP000291106};
RN [1] {ECO:0000313|EMBL:QBF84584.1, ECO:0000313|Proteomes:UP000291106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D4-2 {ECO:0000313|EMBL:QBF84584.1,
RC ECO:0000313|Proteomes:UP000291106};
RA Baek K.;
RT "Shewanella sp. D4-2 isolated from Dokdo Island.";
RL Submitted (FEB-2019) 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}.
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DR EMBL; CP036200; QBF84584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PM35; -.
DR KEGG; smai:EXU30_19345; -.
DR OrthoDB; 2489132at2; -.
DR Proteomes; UP000291106; Chromosome.
DR GO; GO:0005886; C:plasma 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 Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
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 Pfam; PF17200; sCache_2; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM01049; Cache_2; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 217..271
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 276..512
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 319..367
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 548 AA; 60063 MW; C8FC71A0C929927A CRC64;
MNAITLYFRK TTIANRLLFM VALAIIATLL IFGFAVNKVE QYLVDEKQSK LTSLVEVAHT
VVEQYRQHAV SGSMTEEQAK AAAITKLNSL RYSDNDYYFS INDQGVMIQH PFSKKLVGTN
VRQLKDPNGV MLFDEMIVKT RSAQTARVDY MWNKPNQDKP SPKMSMVIKH QAWGWIIGTG
VYVDDIDVAV WDFIWEYLGL LIAVWIPVFL LLYVIMVSIA SPMKQTIEAF ENIARGEGDL
TLRLSQEGSD ELKQIAEYFN LFTEKIQQLV KSVSELVVDS SDLAANLSNI ANTANDISTN
VQAETEGVAT AVNQMAVTAT DVAANAQDAN HTVKSAENET TTASLAVSSA MDRINSLSQE
LEHTEQMTHS LTVSSSEIGQ ILEVIVGIAE QTNLLALNAA IEAARAGEAG RGFAVVADEV
RTLASRTQDS TQQINNIIEA IRSSVASVNA SVVKAKASSS ETVSETATVV DVLEQVKASI
LQISDMNGHI ANATEEQNRV ISELNVNITR INEMSLENHQ QNALINDNSE QINQGAADLA
KLVDQFKV
//