PAL_ECOLI
ID PAL_ECOLI Reviewed; 173 AA.
AC P0A912; P07176;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000303|PubMed:3545827};
DE Short=PAL {ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000305};
DE AltName: Full=Tol-Pal system lipoprotein Pal {ECO:0000305};
DE Flags: Precursor;
GN Name=pal {ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000303|PubMed:3545827};
GN Synonyms=excC {ECO:0000303|PubMed:1574003};
GN OrderedLocusNames=b0741, JW0731;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-22, AND
RP PALMITOYLATION AT CYS-22.
RC STRAIN=K12;
RX PubMed=3545827; DOI=10.1111/j.1432-1033.1987.tb10738.x;
RA Chen R., Henning U.;
RT "Nucleotide sequence of the gene for the peptidoglycan-associated
RT lipoprotein of Escherichia coli K12.";
RL Eur. J. Biochem. 163:73-77(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=1574003; DOI=10.1111/j.1365-2958.1992.tb01523.x;
RA Lazzaroni J.-C., Portalier R.;
RT "The excC gene of Escherichia coli K-12 required for cell envelope
RT integrity encodes the peptidoglycan-associated lipoprotein (PAL).";
RL Mol. Microbiol. 6:735-742(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RC STRAIN=K12 / JM105 / ATCC 47016;
RX PubMed=2687247; DOI=10.1128/jb.171.12.6600-6609.1989;
RA Levengood S.K., Webster R.E.;
RT "Nucleotide sequences of the tolA and tolB genes and localization of their
RT products, components of a multistep translocation system in Escherichia
RT coli.";
RL J. Bacteriol. 171:6600-6609(1989).
RN [7]
RP INTERACTION WITH TOLB.
RX PubMed=7744736; DOI=10.1074/jbc.270.19.11071;
RA Bouveret E., Derouiche R., Rigal A., Lloubes R., Lazdunski C.,
RA Benedetti H.;
RT "Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to
RT explaining the formation of contact sites between the inner and outer
RT membranes of Escherichia coli.";
RL J. Biol. Chem. 270:11071-11077(1995).
RN [8]
RP INTERACTION WITH TOLB AND OMPA.
RX PubMed=9701827; DOI=10.1046/j.1365-2958.1998.00945.x;
RA Clavel T., Germon P., Vianney A., Portalier R., Lazzaroni J.-C.;
RT "TolB protein of Escherichia coli K-12 interacts with the outer membrane
RT peptidoglycan-associated proteins Pal, Lpp and OmpA.";
RL Mol. Microbiol. 29:359-367(1998).
RN [9]
RP FUNCTION, AND INTERACTION WITH TOLA.
RX PubMed=11115123; DOI=10.1046/j.1365-2958.2000.02190.x;
RA Cascales E., Gavioli M., Sturgis J.N., Lloubes R.;
RT "Proton motive force drives the interaction of the inner membrane TolA and
RT outer membrane pal proteins in Escherichia coli.";
RL Mol. Microbiol. 38:904-915(2000).
RN [10]
RP INTERACTION WITH TOLA.
RX PubMed=11722743; DOI=10.1046/j.1365-2958.2001.02673.x;
RA Cascales E., Lloubes R., Sturgis J.N.;
RT "The TolQ-TolR proteins energize TolA and share homologies with the
RT flagellar motor proteins MotA-MotB.";
RL Mol. Microbiol. 42:795-807(2001).
RN [11]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17233825; DOI=10.1111/j.1365-2958.2006.05571.x;
RA Gerding M.A., Ogata Y., Pecora N.D., Niki H., de Boer P.A.;
RT "The trans-envelope Tol-Pal complex is part of the cell division machinery
RT and required for proper outer-membrane invagination during cell
RT constriction in E. coli.";
RL Mol. Microbiol. 63:1008-1025(2007).
RN [12]
RP FUNCTION.
RX PubMed=24720726; DOI=10.1111/mmi.12609;
RA Santos T.M., Lin T.Y., Rajendran M., Anderson S.M., Weibel D.B.;
RT "Polar localization of Escherichia coli chemoreceptors requires an intact
RT Tol-Pal complex.";
RL Mol. Microbiol. 92:985-1004(2014).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32152098; DOI=10.1073/pnas.1919267117;
RA Yakhnina A.A., Bernhardt T.G.;
RT "The Tol-Pal system is required for peptidoglycan-cleaving enzymes to
RT complete bacterial cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:6777-6783(2020).
RN [14] {ECO:0007744|PDB:1OAP}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 65-173.
RX PubMed=11173492; DOI=10.1107/s0907444900019739;
RA Abergel C., Walburger A., Chenivesse S., Lazdunski C.;
RT "Crystallization and preliminary crystallographic study of the
RT peptidoglycan-associated lipoprotein from Escherichia coli.";
RL Acta Crystallogr. D 57:317-319(2001).
RN [15] {ECO:0007744|PDB:2HQS}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 64-173 IN COMPLEX WITH TOLB.
RX PubMed=17375930; DOI=10.1021/ja070153n;
RA Bonsor D.A., Grishkovskaya I., Dodson E.J., Kleanthous C.;
RT "Molecular mimicry enables competitive recruitment by a natively disordered
RT protein.";
RL J. Am. Chem. Soc. 129:4800-4807(2007).
RN [16] {ECO:0007744|PDB:2W8B}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 64-173 IN COMPLEX WITH TOLB.
RX PubMed=19696740; DOI=10.1038/emboj.2009.224;
RA Bonsor D.A., Hecht O., Vankemmelbeke M., Sharma A., Krachler A.M.,
RA Housden N.G., Lilly K.J., James R., Moore G.R., Kleanthous C.;
RT "Allosteric beta-propeller signalling in TolB and its manipulation by
RT translocating colicins.";
RL EMBO J. 28:2846-2857(2009).
CC -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC membrane invagination during cell division and is important for
CC maintaining outer membrane integrity (PubMed:11115123,
CC PubMed:17233825). The Tol-Pal system is also required for polar
CC localization of chemoreceptors clusters (PubMed:24720726). The system
CC also appears to be required for the activity of several outer membrane-
CC localized enzymes with cell wall remodeling activity (PubMed:32152098).
CC {ECO:0000269|PubMed:11115123, ECO:0000269|PubMed:17233825,
CC ECO:0000269|PubMed:24720726, ECO:0000269|PubMed:32152098}.
CC -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC TolB and the outer membrane protein Pal. They form a network linking
CC the inner and outer membranes and the peptidoglycan layer
CC (PubMed:17233825). Pal interacts with TolB (PubMed:7744736,
CC PubMed:17375930, PubMed:19696740). Interacts with the C-terminal domain
CC of TolA. This interaction is proton motive force dependent and requires
CC TolQ and TolR (PubMed:11115123, PubMed:11722743). Can form a complex
CC with TolB and OmpA (PubMed:9701827). {ECO:0000269|PubMed:11115123,
CC ECO:0000269|PubMed:11722743, ECO:0000269|PubMed:17375930,
CC ECO:0000269|PubMed:19696740, ECO:0000269|PubMed:7744736,
CC ECO:0000269|PubMed:9701827, ECO:0000305|PubMed:17233825}.
CC -!- INTERACTION:
CC P0A912; P61316: lolA; NbExp=2; IntAct=EBI-1124760, EBI-553532;
CC P0A912; P61320: lolB; NbExp=2; IntAct=EBI-1124760, EBI-1122794;
CC P0A912; P75958: lolE; NbExp=2; IntAct=EBI-1124760, EBI-1125190;
CC P0A912; P0A855: tolB; NbExp=4; IntAct=EBI-1124760, EBI-7180728;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02204, ECO:0000269|PubMed:1574003}; Lipid-anchor
CC {ECO:0000255|HAMAP-Rule:MF_02204, ECO:0000269|PubMed:1574003}.
CC Note=Accumulates at cell constriction sites. Recruitment to the
CC division site is dependent on FtsN activity.
CC {ECO:0000269|PubMed:17233825}.
CC -!- DISRUPTION PHENOTYPE: Mutants lacking the tol-pal cluster suffer
CC delayed outer membrane invagination and contain large outer membrane
CC blebs at constriction sites and cell poles (PubMed:17233825). Tol-pal
CC mutants fail to complete division and form cell chains, and fail to
CC process denuded peptidoglycans at the septum (PubMed:32152098).
CC {ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:32152098}.
CC -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_02204, ECO:0000305}.
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DR EMBL; X05123; CAA28771.1; -; Genomic_DNA.
DR EMBL; X65796; CAA46673.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73835.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35407.1; -; Genomic_DNA.
DR EMBL; M28232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A27534; LPECPG.
DR RefSeq; NP_415269.1; NC_000913.3.
DR RefSeq; WP_001295306.1; NZ_STEB01000035.1.
DR PDB; 1OAP; X-ray; 1.93 A; A=65-173.
DR PDB; 2HQS; X-ray; 1.50 A; C/E/G/H=65-173.
DR PDB; 2W8B; X-ray; 1.86 A; C/E/G/H=65-173.
DR PDBsum; 1OAP; -.
DR PDBsum; 2HQS; -.
DR PDBsum; 2W8B; -.
DR AlphaFoldDB; P0A912; -.
DR SMR; P0A912; -.
DR BioGRID; 4260724; 260.
DR BioGRID; 849398; 1.
DR ComplexPortal; CPX-5782; Tol-Pal cell envelope complex.
DR DIP; DIP-51001N; -.
DR IntAct; P0A912; 9.
DR MINT; P0A912; -.
DR STRING; 511145.b0741; -.
DR jPOST; P0A912; -.
DR PaxDb; P0A912; -.
DR PRIDE; P0A912; -.
DR EnsemblBacteria; AAC73835; AAC73835; b0741.
DR EnsemblBacteria; BAA35407; BAA35407; BAA35407.
DR GeneID; 66670989; -.
DR GeneID; 945004; -.
DR KEGG; ecj:JW0731; -.
DR KEGG; eco:b0741; -.
DR PATRIC; fig|1411691.4.peg.1531; -.
DR EchoBASE; EB0678; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016890_9_4_6; -.
DR InParanoid; P0A912; -.
DR OMA; MNQGEET; -.
DR PhylomeDB; P0A912; -.
DR BioCyc; EcoCyc:EG10684-MON; -.
DR EvolutionaryTrace; P0A912; -.
DR PRO; PR:P0A912; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0031246; C:intrinsic component of periplasmic side of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IDA:EcoCyc.
DR GO; GO:1905153; P:regulation of membrane invagination; IC:ComplexPortal.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR HAMAP; MF_02204; Pal; 1.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR039001; Pal.
DR InterPro; IPR014169; Pal_lipo_C.
DR Pfam; PF00691; OmpA; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR TIGRFAMs; TIGR02802; Pal_lipo; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell outer membrane; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT CHAIN 22..173
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT /id="PRO_0000020120"
FT DOMAIN 60..173
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT REGION 30..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204,
FT ECO:0000269|PubMed:3545827"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204,
FT ECO:0000305|PubMed:3545827"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 115..135
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2HQS"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:2HQS"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2HQS"
SQ SEQUENCE 173 AA; 18824 MW; 449F9959C0274430 CRC64;
MQLNKVLKGL MIALPVMAIA ACSSNKNASN DGSEGMLGAG TGMDANGGNG NMSSEEQARL
QMQQLQQNNI VYFDLDKYDI RSDFAQMLDA HANFLRSNPS YKVTVEGHAD ERGTPEYNIS
LGERRANAVK MYLQGKGVSA DQISIVSYGK EKPAVLGHDE AAYSKNRRAV LVY
