AOAH_MOUSE
ID AOAH_MOUSE Reviewed; 574 AA.
AC O35298;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Acyloxyacyl hydrolase {ECO:0000303|Ref.1};
DE EC=3.1.1.77 {ECO:0000305|PubMed:12810692, ECO:0000305|PubMed:15155618, ECO:0000305|PubMed:17322564, ECO:0000305|PubMed:18779055, ECO:0000305|PubMed:19860560};
DE Contains:
DE RecName: Full=Acyloxyacyl hydrolase small subunit {ECO:0000250|UniProtKB:P28039};
DE Contains:
DE RecName: Full=Acyloxyacyl hydrolase large subunit {ECO:0000250|UniProtKB:P28039};
DE Flags: Precursor;
GN Name=Aoah {ECO:0000303|PubMed:15155618};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57B1/6;
RA Munford R.S., Fosmire S., Varley A.W., Staab J.F.;
RT "Human, murine, and lapine acyloxyacyl hydrolases share unique structural
RT features.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12810692; DOI=10.1084/jem.20030420;
RA Lu M., Zhang M., Kitchens R.L., Fosmire S., Takashima A., Munford R.S.;
RT "Stimulus-dependent deacylation of bacterial lipopolysaccharide by
RT dendritic cells.";
RL J. Exp. Med. 197:1745-1754(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15155618; DOI=10.1128/iai.72.6.3171-3178.2004;
RA Feulner J.A., Lu M., Shelton J.M., Zhang M., Richardson J.A., Munford R.S.;
RT "Identification of acyloxyacyl hydrolase, a lipopolysaccharide-detoxifying
RT enzyme, in the murine urinary tract.";
RL Infect. Immun. 72:3171-3178(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17322564; DOI=10.1074/jbc.m609462200;
RA Shao B., Lu M., Katz S.C., Varley A.W., Hardwick J., Rogers T.E.,
RA Ojogun N., Rockey D.C., Dematteo R.P., Munford R.S.;
RT "A host lipase detoxifies bacterial lipopolysaccharides in the liver and
RT spleen.";
RL J. Biol. Chem. 282:13726-13735(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18779055; DOI=10.1016/j.chom.2008.06.009;
RA Lu M., Varley A.W., Ohta S., Hardwick J., Munford R.S.;
RT "Host inactivation of bacterial lipopolysaccharide prevents prolonged
RT tolerance following gram-negative bacterial infection.";
RL Cell Host Microbe 4:293-302(2008).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19860560; DOI=10.1086/646616;
RA Ojogun N., Kuang T.Y., Shao B., Greaves D.R., Munford R.S., Varley A.W.;
RT "Overproduction of acyloxyacyl hydrolase by macrophages and dendritic cells
RT prevents prolonged reactions to bacterial lipopolysaccharide in vivo.";
RL J. Infect. Dis. 200:1685-1693(2009).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28622363; DOI=10.1371/journal.ppat.1006436;
RA Zou B., Jiang W., Han H., Li J., Mao W., Tang Z., Yang Q., Qian G.,
RA Qian J., Zeng W., Gu J., Chu T., Zhu N., Zhang W., Yan D., He R., Chu Y.,
RA Lu M.;
RT "Acyloxyacyl hydrolase promotes the resolution of lipopolysaccharide-
RT induced acute lung injury.";
RL PLoS Pathog. 13:E1006436-E1006436(2017).
RN [9] {ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-574 OF MUTANT ALA-262 IN
RP COMPLEX WITH CALCIUM AND THE LIPID A MOIETY OF BACTERIAL
RP LIPOPOLYSACCHARIDE, COFACTOR, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF
RP SER-262, ACTIVE SITE, AND GLYCOSYLATION AT ASN-206; ASN-408 AND ASN-465.
RX PubMed=29343645; DOI=10.1073/pnas.1719834115;
RA Gorelik A., Illes K., Nagar B.;
RT "Crystal structure of the mammalian lipopolysaccharide detoxifier.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E896-E905(2018).
CC -!- FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains
CC from the lipid A region of bacterial lipopolysaccharides (LPS)
CC (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560).
CC By breaking down LPS, terminates the host response to bacterial
CC infection and prevents prolonged and damaging inflammatory responses
CC (PubMed:17322564, PubMed:19860560, PubMed:28622363). In peritoneal
CC macrophages, seems to be important for recovery from a state of immune
CC tolerance following infection by Gram-negative bacteria
CC (PubMed:18779055). {ECO:0000269|PubMed:12810692,
CC ECO:0000269|PubMed:15155618, ECO:0000269|PubMed:17322564,
CC ECO:0000269|PubMed:18779055, ECO:0000269|PubMed:19860560,
CC ECO:0000269|PubMed:28622363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-
CC hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+);
CC Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675;
CC EC=3.1.1.77; Evidence={ECO:0000305|PubMed:12810692,
CC ECO:0000305|PubMed:15155618, ECO:0000305|PubMed:17322564,
CC ECO:0000305|PubMed:18779055, ECO:0000305|PubMed:19860560};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:29343645};
CC Note=Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a
CC structural role. {ECO:0000269|PubMed:29343645};
CC -!- SUBUNIT: Heterodimer of the large and small subunits; disulfide-linked.
CC {ECO:0000305|PubMed:15155618, ECO:0000305|PubMed:29343645}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15155618}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in
CC urine. {ECO:0000269|PubMed:15155618}.
CC -!- TISSUE SPECIFICITY: Detected in peritoneal macrophages (at protein
CC level) (PubMed:17322564, PubMed:28622363). Strongly expressed in kidney
CC cortex, where it may be produced by proximal tubule cells
CC (PubMed:15155618). In liver, expressed at high levels in Kupffer cells
CC (PubMed:17322564). Expressed by dendritic cells (PubMed:12810692).
CC Detected at low levels in alveolar macrophages (PubMed:28622363).
CC {ECO:0000269|PubMed:12810692, ECO:0000269|PubMed:15155618,
CC ECO:0000269|PubMed:17322564, ECO:0000269|PubMed:28622363}.
CC -!- INDUCTION: Strongly up-regulated in alveolar macrophages in response to
CC bacterial lipopolysaccharides (LPS). {ECO:0000269|PubMed:28622363}.
CC -!- PTM: Cleaved into a large and a small subunit.
CC {ECO:0000250|UniProtKB:P28039}.
CC -!- PTM: The small subunit is N-glycosylated.
CC {ECO:0000250|UniProtKB:P28039}.
CC -!- DISRUPTION PHENOTYPE: Animals develop significant and prolonged
CC hepatosplenomegaly in response to bacterial lipopolysaccharide (LPS)
CC challenge (PubMed:17322564). Both liver and spleen show increased
CC accumulation of leukocytes (PubMed:17322564). Significantly reduced
CC deacylation of LPS in liver and spleen, in peritoneal macrophages, and
CC in bone marrow-derived dendritic cells (PubMed:12810692,
CC PubMed:17322564, PubMed:18779055). Increased lung injury, delayed
CC neutrophil clearance, and prolonged recovery time in response to
CC intranasal LPS administration (PubMed:28622363). Alveolar macrophages
CC show persistent activation and cytokine levels in lung remain elevated
CC 4-7 days after LPS administration (PubMed:28622363). Impaired response
CC to a second infection challenge, with reduced production of the pro-
CC inflammatory chemokines CCL5/RANTES, TNF and IL6 by peritoneal
CC macrophages and reduced survival rates, indicating a prolonged state of
CC immune tolerance (PubMed:18779055). This immune tolerant state can
CC perisist for two months or longer (PubMed:18779055).
CC {ECO:0000269|PubMed:12810692, ECO:0000269|PubMed:17322564,
CC ECO:0000269|PubMed:18779055, ECO:0000269|PubMed:28622363}.
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DR EMBL; AF018172; AAB81182.1; -; mRNA.
DR EMBL; AK084452; BAC39187.1; -; mRNA.
DR CCDS; CCDS26266.1; -.
DR RefSeq; NP_001268783.1; NM_001281854.1.
DR RefSeq; NP_036184.1; NM_012054.4.
DR PDB; 5W7D; X-ray; 1.75 A; A=23-574.
DR PDB; 5W7E; X-ray; 1.83 A; A/B=23-574.
DR PDB; 5W7F; X-ray; 2.80 A; A/B=23-574.
DR PDBsum; 5W7D; -.
DR PDBsum; 5W7E; -.
DR PDBsum; 5W7F; -.
DR AlphaFoldDB; O35298; -.
DR SMR; O35298; -.
DR STRING; 10090.ENSMUSP00000021757; -.
DR GlyGen; O35298; 4 sites.
DR iPTMnet; O35298; -.
DR PhosphoSitePlus; O35298; -.
DR MaxQB; O35298; -.
DR PaxDb; O35298; -.
DR PRIDE; O35298; -.
DR ProteomicsDB; 296260; -.
DR Antibodypedia; 26560; 150 antibodies from 24 providers.
DR DNASU; 27052; -.
DR Ensembl; ENSMUST00000021757; ENSMUSP00000021757; ENSMUSG00000021322.
DR GeneID; 27052; -.
DR KEGG; mmu:27052; -.
DR UCSC; uc007ppu.2; mouse.
DR CTD; 313; -.
DR MGI; MGI:1350928; Aoah.
DR VEuPathDB; HostDB:ENSMUSG00000021322; -.
DR eggNOG; ENOG502QVQW; Eukaryota.
DR GeneTree; ENSGT00390000008427; -.
DR HOGENOM; CLU_025769_0_0_1; -.
DR InParanoid; O35298; -.
DR OMA; AGQPFCH; -.
DR OrthoDB; 692811at2759; -.
DR PhylomeDB; O35298; -.
DR TreeFam; TF329246; -.
DR BRENDA; 3.1.1.77; 3474.
DR BioGRID-ORCS; 27052; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Aoah; mouse.
DR PRO; PR:O35298; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O35298; protein.
DR Bgee; ENSMUSG00000021322; Expressed in granulocyte and 57 other tissues.
DR ExpressionAtlas; O35298; baseline and differential.
DR Genevisible; O35298; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0050528; F:acyloxyacyl hydrolase activity; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0009104; P:lipopolysaccharide catabolic process; ISS:UniProtKB.
DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IDA:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:MGI.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR039676; AOAH.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR15010; PTHR15010; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR Pfam; PF03489; SapB_2; 1.
DR SMART; SM00741; SapB; 1.
DR SUPFAM; SSF47862; SSF47862; 1.
DR PROSITE; PS50015; SAP_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid metabolism; Metal-binding; Reference proteome; Secreted;
KW Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P28039"
FT PROPEP 23..33
FT /evidence="ECO:0000250|UniProtKB:P28039"
FT /id="PRO_0000041812"
FT CHAIN 34..155
FT /note="Acyloxyacyl hydrolase small subunit"
FT /evidence="ECO:0000250|UniProtKB:P28039"
FT /id="PRO_0000041813"
FT CHAIN 156..574
FT /note="Acyloxyacyl hydrolase large subunit"
FT /evidence="ECO:0000250|UniProtKB:P28039"
FT /id="PRO_0000041814"
FT DOMAIN 36..117
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT REGION 37..69
FT /note="Important for enzyme activity, localization to
FT cytoplasmic vesicles, and protein stability"
FT /evidence="ECO:0000250|UniProtKB:P28039"
FT REGION 172..176
FT /note="Lipopolysaccharide binding"
FT /evidence="ECO:0000250|UniProtKB:O18823"
FT ACT_SITE 262
FT /evidence="ECO:0000305|PubMed:29343645"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT SITE 344
FT /note="Interacts with lipopolysaccharide"
FT /evidence="ECO:0000250|UniProtKB:O18823"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7E"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7F"
FT DISULFID 40..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D,
FT ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"
FT DISULFID 43..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D,
FT ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"
FT DISULFID 69..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W7D,
FT ECO:0007744|PDB:5W7E, ECO:0007744|PDB:5W7F"
FT DISULFID 122..452
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT DISULFID 122..452
FT /note="Interchain (between small and large subunit)"
FT /evidence="ECO:0000250|UniProtKB:O18823"
FT DISULFID 159..168
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT DISULFID 205..229
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT DISULFID 248..328
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT DISULFID 375..458
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W7D, ECO:0007744|PDB:5W7E,
FT ECO:0007744|PDB:5W7F"
FT MUTAGEN 262
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29343645"
FT HELIX 36..57
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 78..97
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 164..176
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 243..248
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 262..266
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 388..405
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 436..439
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 443..452
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 466..487
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 493..500
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 504..513
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:5W7D"
FT STRAND 527..530
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 532..549
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 551..554
FT /evidence="ECO:0007829|PDB:5W7D"
FT HELIX 561..568
FT /evidence="ECO:0007829|PDB:5W7D"
FT TURN 569..572
FT /evidence="ECO:0007829|PDB:5W7D"
SQ SEQUENCE 574 AA; 65155 MW; 10B32C3BE772FB68 CRC64;
MKFPWKVFKT TLLLLLLSHS LASVPSEDQP GDSYSHGQSC LGCVVLVSVI EQLAEVHNSS
VQVAMERLCS YLPEKLFLKT ACYFLVQTFG SDIIKLLDEA MKADVVCYAL EFCKRGAVQP
QCHLYPLPQE AWESALEKAR QVLRRSSTMK YPRSGRNICS LPFLTKICQK IELSIKKAVP
FKDIDSDKHS VFPTLRGYHW RGRDCNDSDK TVYPGRRPDN WDIHQDSNCN GIWGIDPKDG
IPYEKKFCEG SQPRGIILLG DSAGAHFHIP PEWLTASQMS VNSFLNLPSA LTDELNWPQL
SGVTGFLDST SGIEEKSIYH RLRKRNHCNH RDYQSISKNG ASSRNLKNFI ESLSRNQASD
HPAIVLYAMI GNDVCNSKAD TVPEMTTPEQ MYANVMQTLT HLNSHLPNGS HVILYGLPDG
TFLWDSLHNR YHPLGQLNKD VTYAQFFSFL RCLQLNPCNG WMSSNKTLRT LTSERAEQLS
NTLKKIATTE TFANFDLFYV DFAFHEIIED WQKRGGQPWQ LIEPVDGFHP NEVASLLQAN
RVWEKIQLQW PHVLGKENPF NSQIEEVFGD QGGH
