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Database: UniProt
Entry: A0A136HGX4_9GAMM
LinkDB: A0A136HGX4_9GAMM
Original site: A0A136HGX4_9GAMM 
ID   A0A136HGX4_9GAMM        Unreviewed;       614 AA.
AC   A0A136HGX4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KXJ54828.1};
GN   ORFNames=AXW15_08095 {ECO:0000313|EMBL:KXJ54828.1};
OS   Neptuniibacter sp. Phe_28.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Neptuniibacter.
OX   NCBI_TaxID=1795871 {ECO:0000313|EMBL:KXJ54828.1, ECO:0000313|Proteomes:UP000070472};
RN   [1] {ECO:0000313|Proteomes:UP000070472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) 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:KXJ54828.1}.
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DR   EMBL; LSMR01000101; KXJ54828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136HGX4; -.
DR   Proteomes; UP000070472; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00062; PBPb; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          35..286
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   614 AA;  68410 MW;  A9F35CB509ECB59B CRC64;
     MTLFNKLFGR SQNATWDTQA PMTHAPDPHI DTPYFSDDEK RFYRALQLIS NQTAQLSRQI
     FRALEAQENF LSEINQRATK LDTELNVAND YLNSSNAQVS SLQQQIKTEV DEVNSSISQS
     LDEISSALAN KSSNVSEVLD GILKIGKGIN LLALNASIEA ARAGEHGRGF SVVADEVRRL
     ANVTTEQANQ AAEQLDFSQV NAELSNISAA NTEKLDNFVQ VTQSATEQLT ELFNSIATQL
     SAVMENTAVI FETLEMSNGS MQRISNKNQL INHVVEDMSK GLDQVDIHST DIHLASRAIN
     QTLNKLHLVA DAGHDQLDDV LRRGKLRVAI EPSFVGLSFR EKLGEPLKGL DVDYALAFAR
     YLGVECEFIE APWDMCTELL TSGKKFGQPP ADIVISALPP SAEYDNVAYS EAYTYLPWVL
     ARRKGDHRIN SIQDLQDKVV GVINDPAALM ILEDLGIRWS SNEKKPGGSI TLNNLIAYSD
     QSRIHHCLAD GIVDAFGIDL PIYYWACKNP ASPWYDKIEI IPGNLAPRPF FYTMVVNSSA
     SSYRLLAQAN RFIHWFKQQR ERTAIEQTWQ GTALNGDGSY RDEPGNLLGE SELKTRYEAH
     CHKFNLEPKP LKAQ
//
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