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Database: UniProt
Entry: A0A1H9JZ20_9BURK
LinkDB: A0A1H9JZ20_9BURK
Original site: A0A1H9JZ20_9BURK 
ID   A0A1H9JZ20_9BURK        Unreviewed;       755 AA.
AC   A0A1H9JZ20;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Twitching motility protein PilJ {ECO:0000313|EMBL:SEQ92018.1};
GN   ORFNames=SAMN02982919_01392 {ECO:0000313|EMBL:SEQ92018.1};
OS   Giesbergeria anulus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Giesbergeria.
OX   NCBI_TaxID=180197 {ECO:0000313|EMBL:SEQ92018.1, ECO:0000313|Proteomes:UP000199766};
RN   [1] {ECO:0000313|EMBL:SEQ92018.1, ECO:0000313|Proteomes:UP000199766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35958 {ECO:0000313|EMBL:SEQ92018.1,
RC   ECO:0000313|Proteomes:UP000199766};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOGD01000003; SEQ92018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9JZ20; -.
DR   STRING; 180197.SAMN02982919_01392; -.
DR   OrthoDB; 9177152at2; -.
DR   Proteomes; UP000199766; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF13675; PilJ; 2.
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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199766};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        87..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          429..477
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          482..718
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          397..434
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   755 AA;  80535 MW;  E0C025F8990F4780 CRC64;
     MSVVTKLGSM FSRQPAKTDG AAEQDSLVGA SLDSNLREVF PEEALNSVQM EHNGGYGGEA
     TDQPSPGELI DLPLLGPAVA ASHQRRLLIL LAIGVVVVAL IAGWVLRQAD SAAQQLAATG
     QALMQSQRLA KSVSQALVGS NQAFADVQES AGVLARNVRA LKEGDSELGV QSLGEPFKPE
     LDAIAPLIEH ADHNAGVVMG QQKILTQVGD ALRTVNRQSS DLLEIAETIV ALKIQQNSSA
     AEIFGAGQLV MLTQRIGKSA NEFQTTEGVS PEAVFLLGKD LNSFKEISQG LLDGNTELSL
     PAARDRQTRE YLQSLINLYE QTRVQASAIL GNLQGLVSAR EAQNAIIGES EPLRRHLEGL
     QTKLSAQTGM GMGQFAALLL AATFVVLCGV GISRVQLLDS RNRQQAAELQ NKNAQRQEQE
     AKRINDANQA AILRLMNELQ SVAEGDLTQE ATVTEDITGA IADSVNYTVE ELRVLVGSVQ
     NTATRVAQTT AQVDSTSTEL LAASTEQLRE IRETGRSVLE MASRINEVST QAQESATVAR
     QSLQAADSGL QAVQNAIGGM NAIRDQIQDT SKRIKRLGES SQEIGEITEL ISDITEQTNV
     LALNAAIQAA SAGEAGRGFS VVAEEVQRLA ERSADATRQI SALVKAIQTD TQDAVAAMER
     STQGVVEGAR LSDSAGTALS EIDQVSRRLA ELIEQISSET SSEATLANEM AENIQHIFAV
     TEQTGEGTRT TAQQVRELSH MAEELRQSVA RFKIA
//
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