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 27-MAR-2024, entry version 122.
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; Pseudomonadota; 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}.
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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 PDB; 7ZJR; X-ray; 2.50 A; A=36-309.
DR PDBsum; 7ZJR; -.
DR AlphaFoldDB; P42257; -.
DR SMR; P42257; -.
DR STRING; 208964.PA0411; -.
DR PaxDb; 208964-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 OrthoDB; 9177152at2; -.
DR PhylomeDB; P42257; -.
DR BioCyc; PAER208964:G1FZ6-415-MONOMER; -.
DR Proteomes; UP000002438; Chromosome.
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 CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
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; 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; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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"
FT HELIX 46..72
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 77..98
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 113..134
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 137..170
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 175..199
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 205..228
FT /evidence="ECO:0007829|PDB:7ZJR"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:7ZJR"
FT HELIX 241..302
FT /evidence="ECO:0007829|PDB:7ZJR"
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
//
