ID A0A2A4Z4H2_9PROT Unreviewed; 685 AA.
AC A0A2A4Z4H2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chemotaxis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COB13_06965 {ECO:0000313|EMBL:PCJ01903.1};
OS OCS116 cluster bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; OCS116 cluster.
OX NCBI_TaxID=2030921 {ECO:0000313|EMBL:PCJ01903.1, ECO:0000313|Proteomes:UP000218076};
RN [1] {ECO:0000313|Proteomes:UP000218076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PCJ01903.1}.
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; NVUS01000006; PCJ01903.1; -; Genomic_DNA.
DR Proteomes; UP000218076; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR013587; Nitrate/nitrite_sensing.
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; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF08376; NIT; 1.
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 Coiled coil {ECO:0000256|SAM:Coils}; 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 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..387
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 403..664
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 580..642
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT COILED 376..409
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 685 AA; 74110 MW; 7916379BBB9114E7 CRC64;
MQFLSKMKIS HMIMILVVLP LLALTYFASQ LVLEEYQKNK AMSELGELTQ LAVKLSNLVH
EQQKERGATA IFVGSAGKXF GXELXTQRQN TDKFRQELXA YLXAHESNIY GVEFENYLNL
LLKELGMMST IRDQVDELSL SKADAIGYYT RLNAQNLRFI DEIGQLSQDP NITSAYISYT
SFLQSKERAG IERAVGAGGL SDGKFSLVAI DQFKSLITVQ DTYNTLFVTQ ATNEQVALFN
KFKADSKISD ANAMRDIIIA GGXQGDFKQL TSKIWFDTIT YKINELKKIE NVLSATLLTD
IAGLESSANA GLWXVGIITL ISFIIIICLS FXIIRSINKS FGNIIARMNE LAAGDLDVDL
PAEADNEIGQ MIKCVLVFKN NAIEKVQLEA KQEEDKQXAX XEKQAMMNKM ADDFDADVGG
IVNNVSTASK QLQDTAKMMS KISQTTSXNA TLVANASEIA NNNVQSVAAA SEEMSQSVVE
INQQVTSATK ASKSAVEEVN KTSEEMKNLA TTVEKIGGVV SLIASIADQT NLLALNATIE
SARAGEAGRG FAIVASEVKG LASKTAEATD EISAHILEVH NATQQALSSM DGIGNVIAEI
EQISSSIAMA VDQQGHATQE ISSNAQEAAN GTQEVSHNIG AVTNASQEAD AASNEVMVSA
TKLLEQSNAL KDEVKKFTDE VRSTG
//
