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Database: UniProt
Entry: K9GLI4_9PROT
LinkDB: K9GLI4_9PROT
Original site: K9GLI4_9PROT 
ID   K9GLI4_9PROT            Unreviewed;       490 AA.
AC   K9GLI4;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EKV26870.1};
GN   ORFNames=C882_2093 {ECO:0000313|EMBL:EKV26870.1};
OS   Caenispirillum salinarum AK4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Caenispirillum.
OX   NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV26870.1, ECO:0000313|Proteomes:UP000009881};
RN   [1] {ECO:0000313|EMBL:EKV26870.1, ECO:0000313|Proteomes:UP000009881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK4 {ECO:0000313|EMBL:EKV26870.1,
RC   ECO:0000313|Proteomes:UP000009881};
RX   PubMed=23409257;
RA   Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT   "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT   AK4(T), Isolated from a Solar Saltern.";
RL   Genome Announc. 1:E00199-12(2013).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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:EKV26870.1}.
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DR   EMBL; ANHY01000022; EKV26870.1; -; Genomic_DNA.
DR   RefSeq; WP_009542489.1; NZ_ANHY01000022.1.
DR   AlphaFoldDB; K9GLI4; -.
DR   STRING; 1238182.C882_2093; -.
DR   PATRIC; fig|1238182.3.peg.4047; -.
DR   eggNOG; COG0840; Bacteria.
DR   Proteomes; UP000009881; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR32089:SF112; METHYL-ACCEPTING CHEMOTAXIS PROTEIN CTPH; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
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; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009881};
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          228..450
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   DOMAIN          380..442
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          233..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  50387 MW;  D384CCBEA02A84C6 CRC64;
     MTALDTLRRR YAALLVIALW IMVPVVALTA GLNGVPWLPP AAVGAALALG VTLTWHRDPA
     GLAVRLASGV ALAGVPALLV WSMRGGTWQL DMHMTFFAAL ALAALWCDWR AVATTAAVTA
     VHHLLLNFLM PSLVFPGGAD FGRVVLHAVV VVVQAGALMW LCEQLRRAFV DADAAVVAAK
     AAESQAEAGA AEQAALRHEQ EKVAAALAEA TADFDRRVTQ AVSDLAAAAG ALEDSSETMS
     GTADTTAGRS RSAADESRQA TMNVQTMAAS AEELAASIGE ITRQVARSSE IATGAAEEAR
     RLSATVENLD QAALRIGDVV KLIQDVADQT NLLALNATIE AARAGEAGKG FAVVANEVKA
     LAGQTTRATE DIAAQIAGVQ QVTREAVDAI AGIGTTIGSM DEITAAIAAA VDQQGAATKD
     IARHAEEAAR NTETAAQGID GVSAATDLTR GEAAKVAEAA ESLTGQADGL RAMVDAFLDR
     VRPAQEKAAA
//
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