ID A0A136H8E0_9GAMM Unreviewed; 428 AA.
AC A0A136H8E0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KXJ51705.1};
GN ORFNames=AXW15_04275 {ECO:0000313|EMBL:KXJ51705.1};
OS Neptuniibacter sp. Phe_28.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Neptuniibacter.
OX NCBI_TaxID=1795871 {ECO:0000313|EMBL:KXJ51705.1, 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 -!- 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}.
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:KXJ51705.1}.
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; LSMR01000198; KXJ51705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136H8E0; -.
DR Proteomes; UP000070472; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR004010; Double_Cache_2.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF08269; dCache_2; 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.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
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 74..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..151
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 156..392
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 343..405
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 428 AA; 45912 MW; 85D0720FFE0EAE37 CRC64;
MIVKDLIDHA KGDGGFVRYM WAQPSQNKDA PKLSYAEGLD KWQWMVGTGF YIDDIDNQIL
AAHQKLEDEI ARTLMVLTLV GGGFLVVFGL LAVMFANGIA NPLAKAAAAL TEIAEGGGDL
SKRLDTTAKG EVAEVAYGFN TFAAKIQTLV SEVKSVIDEL SRTSQRMTGV VDETRTEVND
QRRETEQVAA AIHEMAAAVQ EVSTNATNAS HSAQVADESA QGGQQEVNET IVSIELLQGS
VNAASDVIAQ LDRDSEHIGT VINVIKEIAD QTNLLALNAA IEAARAGEQG RGFSVVADEV
RTLATRTQQS TDEIQSMIEK LQAGARKAVH EMEKSRVQTE KTVEKASHTG SKLDHITASV
GDISAMSTQI ATATEEQTAV ADELSRSIQH IADISERASG TADQLADTTS EVSQLEMRLS
ALVNQYKV
//
