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Database: UniProt
Entry: A0A099PAD7_9GAMM
LinkDB: A0A099PAD7_9GAMM
Original site: A0A099PAD7_9GAMM 
ID   A0A099PAD7_9GAMM        Unreviewed;       636 AA.
AC   A0A099PAD7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KGK40986.1};
GN   ORFNames=LH51_18000 {ECO:0000313|EMBL:KGK40986.1};
OS   Nitrincola sp. A-D6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK40986.1, ECO:0000313|Proteomes:UP000029924};
RN   [1] {ECO:0000313|EMBL:KGK40986.1, ECO:0000313|Proteomes:UP000029924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-D6 {ECO:0000313|EMBL:KGK40986.1,
RC   ECO:0000313|Proteomes:UP000029924};
RA   Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA   Fernandez S., Ferrer A., Chavez R., Levican G.;
RT   "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT   Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL   Submitted (SEP-2014) 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:KGK40986.1}.
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DR   EMBL; JRLB01000110; KGK40986.1; -; Genomic_DNA.
DR   RefSeq; WP_036524726.1; NZ_JRLB01000110.1.
DR   AlphaFoldDB; A0A099PAD7; -.
DR   STRING; 1545442.LH51_18000; -.
DR   OrthoDB; 9760371at2; -.
DR   Proteomes; UP000029924; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR029150; dCache_3.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
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; PF14827; dCache_3; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 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   Reference proteome {ECO:0000313|Proteomes:UP000029924};
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..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          305..359
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          364..600
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   DOMAIN          551..613
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
SQ   SEQUENCE   636 AA;  68634 MW;  979D19D3FFA1C573 CRC64;
     MLRNIRISIR LSLGTAIMLA LVIAIIIPTV LNLLSNITQR AESRQLEDLH NALQASIDQT
     AEQALRITTA ATSGVGISEA FANRDRALLQ QLTQPVFEAL QETYNIRQFQ FHQPPATSYL
     RLHQLDKYDD DLSSFRLTVL EANQQQHAQS GLESGVAGIG LRGVIPVYHQ QRHIGSAEVG
     LSFGQDFFNT FTERFGAQAA LHIPADSGFN TFATTIENNT SLSQTQLNQV MQGQVYTSKV
     DRGEQSWAVM ARPIMDFSGK PLGVVELMID RTEYVQGYQQ ALIRIVVIGI VSVLLGLLMA
     TLLARSIIKP LKTTADSLRN IAAGDGDLTA RLDETGRDEL ADLASSFNHF VEHIHSLIKQ
     VGAATVQLSA AAEELSASST DTSQQAKKVQ SETLQVATAM NEMTATVTEV ADNADQTSHA
     AGAANELALS GKQKLVNTQQ SIQGLASDIE AAAQIINHLS NDSREISKIL DVIRDISDQT
     NLLALNAAIE AARAGEQGRG FAVVADEVRS LASRTQNSTV DIQHMIERLQ SGAEKAVNSM
     ELSRSKATTS VTSCNDTNEA LSSIAGAIET INSMNIQIAE AARQQSQVAD EINHNISFIT
     DAAEMTSSST DQVNTAADEL AKLASDLQGR IGRFKV
//
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