ID A0A411PGJ3_9GAMM Unreviewed; 664 AA.
AC A0A411PGJ3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=HAMP domain-containing protein {ECO:0000313|EMBL:QBF82691.1};
GN ORFNames=EXU30_08310 {ECO:0000313|EMBL:QBF82691.1};
OS Shewanella maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=2520507 {ECO:0000313|EMBL:QBF82691.1, ECO:0000313|Proteomes:UP000291106};
RN [1] {ECO:0000313|EMBL:QBF82691.1, ECO:0000313|Proteomes:UP000291106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D4-2 {ECO:0000313|EMBL:QBF82691.1,
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; QBF82691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411PGJ3; -.
DR KEGG; smai:EXU30_08310; -.
DR OrthoDB; 952521at2; -.
DR Proteomes; UP000291106; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 2.40.10.220; predicted glycosyltransferase like domains; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029095; NarX-like_N.
DR InterPro; IPR009875; PilZ_domain.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13675; PilJ; 1.
DR Pfam; PF07238; PilZ; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF141371; PilZ domain-like; 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};
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 178..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 203..258
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 263..499
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 474..508
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 664 AA; 73886 MW; 01815DCADB296B1C CRC64;
MFKSLSIKQK LFLLPMIIAL ALIGEATLVT YTLMQNESDT SIINIAGRQR MLTKKYSAEE
LFHAEYLDHK MPAPLAASHT VNLYETSLKA LKYGGKTYSD LSMTKPIELP KVDYQPFLEQ
LKVVEGLWQE QLRVAQKLEH DFNLQTADEF LIANHKALGA MNKAVGLFAQ HSRSKLDILI
WESIILAVVI SILCIGFALM IIRNITTTIN LLVGISRKIG EGDLKQDPKL LDAINSNELG
RLAQNIEIMR QSLQDTLGEI QLASSSINLS STQVSDLSSQ INAANHTERQ RFEMIHSNSK
SLDQSTIRLV EITSETLDMA TQCNQLSTEA SELVTKNIAM MKTTSDETEK ATNFIQELSD
TAEQVSGIVD SIRAISEQTN LLALNAAIEA ARAGEQGRGF AVVADEVRGL AARTGDSTDE
IAKLISQLTE GVKLVVNSMG EVSSRVEQSR NTSKQTAEGI IEVTERIQQV ATAQQSIDEQ
VEQQKQQLDE LKNTQIELED IINESHKKSR TSTLVAKQLS KVCIDITEVI QKFSVDVTLN
STKKKDDCNR AHPRVKTGLH YELTQGDKHI QGLTDDISFG GTRLILPAGT HNLDENQTVT
VDIDYLYQGN SKRMRIGGRI IHQHQPKTNK LLLHIDFDTP NASQTQALEE IYFEHQHSGE
FKHG
//
