ID   PILJ_PSEAE              Reviewed;         682 AA.
AC   P42257;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Protein PilJ;
GN   Name=pilJ; OrderedLocusNames=PA0411;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=7908398; DOI=10.1111/j.1365-2958.1994.tb00296.x;
RA   Darzins A.;
RT   "Characterization of a Pseudomonas aeruginosa gene cluster involved in
RT   pilus biosynthesis and twitching motility: sequence similarity to the
RT   chemotaxis proteins of enterics and the gliding bacterium Myxococcus
RT   xanthus.";
RL   Mol. Microbiol. 11:137-153(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: May be a part of a signal-transduction system that regulates
CC       twitching motility by controlling pilus function (extension and
CC       retraction).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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; L22036; AAA25952.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG03800.1; -; Genomic_DNA.
DR   PIR; S40037; S40037.
DR   RefSeq; NP_249102.1; NC_002516.2.
DR   RefSeq; WP_003100940.1; NZ_QZGE01000016.1.
DR   AlphaFoldDB; P42257; -.
DR   SMR; P42257; -.
DR   STRING; 287.DR97_3379; -.
DR   PaxDb; P42257; -.
DR   PRIDE; P42257; -.
DR   EnsemblBacteria; AAG03800; AAG03800; PA0411.
DR   GeneID; 878180; -.
DR   KEGG; pae:PA0411; -.
DR   PATRIC; fig|208964.12.peg.432; -.
DR   PseudoCAP; PA0411; -.
DR   HOGENOM; CLU_000445_107_27_6; -.
DR   InParanoid; P42257; -.
DR   OMA; NTIHGMD; -.
DR   PhylomeDB; P42257; -.
DR   BioCyc; PAER208964:G1FZ6-415-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR029095; NarX-like_N.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF13675; PilJ; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Methylation;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..682
FT                   /note="Protein PilJ"
FT                   /id="PRO_0000110562"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..306
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..682
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          347..398
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          403..639
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ   SEQUENCE   682 AA;  72528 MW;  1088AAF1D7F312B9 CRC64;
     MKKINAGNLF AGMRSSSVIA GLFIVLIVSI VLLFANFAYL NTQSNHDKQY IGHAGELRVL
     SQRIAKNATE AAAGKGEAFK LLKDARNDFE KRWNILVNGD ESTSLPPSPE AVKPQMDVVQ
     QDWDGLRKNA DSILASEQTV LSLHQVASTL AETIPQLQVE YEEVVDILLE NGAPADQVAV
     AQRQSLLAER ILGSVNKVLA GDENSVQAAD SFGRDASLFG RVLKGMQEGN AAMSISKVTN
     AEAVDRLNEI AELFEFVSGS VDEILETSPD LFQVREAANN IFSVSQTLLD KASQLADGFE
     NLAGGRSINL FAGYALGALA LASIILIGLV MVRETNRRLA ETAEKNDRNQ AAILRLLDEI
     ADLADGDLTV AATVTEDFTG AIADSINYSI DQLRELVETI NQTAVQVAAA AQETQSTAMH
     LAEASEHQAQ EIAGASAAIN EMAVSIDQVS ANASESSAVA ERSVAIANKG NEVVHNTITG
     MDNIREQIQD TSKRIKRLGE SSQEIGDIVS LINDIADQTN ILALNAAIQA SMAGDAGRGF
     AVVADEVQRL AERSSAATKQ IEALVKTIQT DTNEAVISME QTTSEVVRGA RLAQDAGVAL
     EEIEKVSKTL AALIQNISNA ARQQASSAGH ISNTMNVIQE ITSQTSAGTT ATARSIGNLA
     KMASEMRNSV SGFKLPEGVE QA