PAL_HAEIN
ID PAL_HAEIN Reviewed; 153 AA.
AC P10324;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Peptidoglycan-associated lipoprotein {ECO:0000255|HAMAP-Rule:MF_02204};
DE Short=PAL {ECO:0000255|HAMAP-Rule:MF_02204};
DE AltName: Full=15 kDa peptidoglycan-associated lipoprotein;
DE Short=PC protein;
DE AltName: Full=Outer membrane protein P6;
DE Short=OMP P6;
DE Flags: Precursor;
GN Name=pal {ECO:0000255|HAMAP-Rule:MF_02204}; Synonyms=ompP6;
GN OrderedLocusNames=HI_0381;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, DIACYLGLYCEROL
RP AT CYS-20, AND PALMITOYLATION AT CYS-20.
RX PubMed=2828309; DOI=10.1128/jb.170.2.489-498.1988;
RA Deich R.A., Metcalf B.J., Finn C.W., Farley J.E., Green B.A.;
RT "Cloning of genes encoding a 15,000-dalton peptidoglycan-associated outer
RT membrane lipoprotein and an antigenically related 15,000-dalton protein
RT from Haemophilus influenzae.";
RL J. Bacteriol. 170:489-498(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3257200; DOI=10.1128/iai.56.1.128-134.1988;
RA Nelson M.B., Apicella M.A., Murphy T.F., Vankeulen H., Spotila L.D.,
RA Rekosh D.;
RT "Cloning and sequencing of Haemophilus influenzae outer membrane protein
RT P6.";
RL Infect. Immun. 56:128-134(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [4]
RP STRUCTURE BY NMR OF 20-153 IN COMPLEX WITH PEPTIDOGLYCAN.
RX PubMed=16475801; DOI=10.1021/bi052227i;
RA Parsons L.M., Lin F., Orban J.;
RT "Peptidoglycan recognition by Pal, an outer membrane lipoprotein.";
RL Biochemistry 45:2122-2128(2006).
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. {ECO:0000255|HAMAP-
CC Rule:MF_02204}.
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 {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_02204}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_02204}.
CC -!- SIMILARITY: Belongs to the Pal lipoprotein family. {ECO:0000255|HAMAP-
CC Rule:MF_02204}.
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DR EMBL; M19391; AAA24994.1; -; Genomic_DNA.
DR EMBL; M18878; AAA24940.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22039.1; -; Genomic_DNA.
DR PIR; A28543; A28543.
DR RefSeq; NP_438542.1; NC_000907.1.
DR RefSeq; WP_005652235.1; NC_000907.1.
DR PDB; 2AIZ; NMR; -; P=20-153.
DR PDBsum; 2AIZ; -.
DR AlphaFoldDB; P10324; -.
DR BMRB; P10324; -.
DR SMR; P10324; -.
DR STRING; 71421.HI_0381; -.
DR Allergome; 7668; Hae in P6.
DR PRIDE; P10324; -.
DR EnsemblBacteria; AAC22039; AAC22039; HI_0381.
DR KEGG; hin:HI_0381; -.
DR PATRIC; fig|71421.8.peg.399; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016890_9_4_6; -.
DR OMA; ESNESCW; -.
DR PhylomeDB; P10324; -.
DR BioCyc; HINF71421:G1GJ1-396-MON; -.
DR EvolutionaryTrace; P10324; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
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;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT CHAIN 20..153
FT /note="Peptidoglycan-associated lipoprotein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT /id="PRO_0000020123"
FT DOMAIN 40..153
FT /note="OmpA-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204"
FT REGION 55..56
FT /note="Peptidoglycan binding"
FT REGION 97..101
FT /note="Peptidoglycan binding"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204,
FT ECO:0000269|PubMed:2828309"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02204,
FT ECO:0000269|PubMed:2828309"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2AIZ"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:2AIZ"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2AIZ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2AIZ"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:2AIZ"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2AIZ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2AIZ"
FT HELIX 95..115
FT /evidence="ECO:0007829|PDB:2AIZ"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2AIZ"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2AIZ"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:2AIZ"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:2AIZ"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2AIZ"
SQ SEQUENCE 153 AA; 16108 MW; 3DF358122EF17A11 CRC64;
MNKFVKSLLV AGSVAALAAC SSSNNDAAGN GAAQTFGGYS VADLQQRYNT VYFGFDKYDI
TGEYVQILDA HAAYLNATPA AKVLVEGNTD ERGTPEYNIA LGQRRADAVK GYLAGKGVDA
GKLGTVSYGE EKPAVLGHDE AAYSKNRRAV LAY
