lamB

Functionⁱ

Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda.

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	31	Greasy slide, important in sugar transport	1
Siteⁱ	66	Greasy slide, important in sugar transport	1
Siteⁱ	99	Greasy slide, important in sugar transport	1
Siteⁱ	143	Important in sugar transport	1
Siteⁱ	252	Greasy slide, important in sugar transport	1
Siteⁱ	383	Greasy slide, important in sugar transport	1
Siteⁱ	445	Greasy slide, important in sugar transport	1

GO - Molecular functionⁱ

carbohydrate transmembrane transporter activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
  Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
  Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
maltodextrin transmembrane transporter activity
Source: EcoCyc
Inferred from direct assayⁱ
- "Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli."
  Luckey M., Nikaido H.
  Proc. Natl. Acad. Sci. U.S.A. 77:167-171(1980) [PubMed] [Europe PMC] [Abstract]
maltose transporting porin activity Source: InterPro
porin activity
Source: CACAO
Inferred from direct assayⁱ
- "Decreased expression of LamB and Odp1 complex is crucial for antibiotic resistance in Escherichia coli."
  Lin X.M., Yang M.J., Li H., Wang C., Peng X.X.
  J Proteomics 98:244-253(2014) [PubMed] [Europe PMC] [Abstract]
virus receptor activity Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Host cell receptor for virus entry, Porin, Receptor
Biological process	Host-virus interaction, Ion transport, Sugar transport, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10528-MONOMER ECOL316407:JW3996-MONOMER MetaCyc:EG10528-MONOMER

BioCycⁱ

EcoCyc:EG10528-MONOMER
ECOL316407:JW3996-MONOMER
MetaCyc:EG10528-MONOMER

Protein family/group databases

TCDBⁱ	1.B.3.1.1 the sugar porin (sp) family

TCDBⁱ

1.B.3.1.1 the sugar porin (sp) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Maltoporin Alternative name(s): Lambda receptor protein Maltose-inducible porin
Gene namesⁱ	Name:lamB Synonyms:malB Ordered Locus Names:b4036, JW3996
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Subcellular locationⁱ

Cell outer membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.13
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
; Multi-pass membrane protein
1 Publication
Manual assertion based on experiment inⁱ
- Ref.13
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	26	Periplasmic	1
Transmembraneⁱ	27 – 35	Beta stranded	9
Topological domainⁱ	36 – 64	ExtracellularAdd BLAST	29
Transmembraneⁱ	65 – 78	Beta strandedAdd BLAST	14
Topological domainⁱ	79 – 80	Periplasmic	2
Transmembraneⁱ	81 – 93	Beta strandedAdd BLAST	13
Topological domainⁱ	94 – 104	ExtracellularAdd BLAST	11
Transmembraneⁱ	105 – 115	Beta strandedAdd BLAST	11
Topological domainⁱ	116 – 122	Periplasmic	7
Transmembraneⁱ	123 – 130	Beta stranded	8
Topological domainⁱ	131 – 148	ExtracellularAdd BLAST	18
Transmembraneⁱ	149 – 159	Beta strandedAdd BLAST	11
Topological domainⁱ	160 – 161	Periplasmic	2
Transmembraneⁱ	162 – 173	Beta strandedAdd BLAST	12
Topological domainⁱ	174 – 191	ExtracellularAdd BLAST	18
Transmembraneⁱ	192 – 205	Beta strandedAdd BLAST	14
Topological domainⁱ	206 – 209	Periplasmic	4
Transmembraneⁱ	210 – 222	Beta strandedAdd BLAST	13
Topological domainⁱ	223 – 234	ExtracellularAdd BLAST	12
Transmembraneⁱ	235 – 248	Beta strandedAdd BLAST	14
Topological domainⁱ	249 – 250	Periplasmic	2
Transmembraneⁱ	251 – 263	Beta strandedAdd BLAST	13
Topological domainⁱ	264 – 290	ExtracellularAdd BLAST	27
Transmembraneⁱ	291 – 305	Beta strandedAdd BLAST	15
Topological domainⁱ	306 – 307	Periplasmic	2
Transmembraneⁱ	308 – 323	Beta strandedAdd BLAST	16
Topological domainⁱ	324 – 326	Extracellular	3
Transmembraneⁱ	327 – 341	Beta strandedAdd BLAST	15
Topological domainⁱ	342 – 343	Periplasmic	2
Transmembraneⁱ	344 – 359	Beta strandedAdd BLAST	16
Topological domainⁱ	360 – 362	Extracellular	3
Transmembraneⁱ	363 – 378	Beta strandedAdd BLAST	16
Topological domainⁱ	379 – 385	Periplasmic	7
Transmembraneⁱ	386 – 400	Beta strandedAdd BLAST	15
Topological domainⁱ	401 – 430	ExtracellularAdd BLAST	30
Transmembraneⁱ	431 – 445	Beta strandedAdd BLAST	15
Topological domainⁱ	446	Periplasmic	1

GO - Cellular componentⁱ

Complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell outer membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	33	R → H: Reduces ligand affinity and pore size, no longer selective for maltodextrins. 1 Publication	1
Mutagenesisⁱ	99	W → R: Decreases starch affinity, slightly increases maltose affinity. 1 Publication	1
Mutagenesisⁱ	107	R → S: Decreases maltodextrin affinity, increases sucrose binding and transport. 1 Publication	1
Mutagenesisⁱ	134	R → A: Considerable increase in pore size and sucrose transport, slight decrease in maltose transport; when associated with A-143. 1 Publication	1
Mutagenesisⁱ	134	R → D or N: Slight increase in pore size; increase in sucrose transport and slight decrease in maltose transport; when associated with D-143 and F-146. 1 Publication	1
Mutagenesisⁱ	143	Y → F: Increases affinity for starch and maltose, pore size and transport of maltohexaose. 2 Publications	1
Mutagenesisⁱ	146	D → G: Increases affinity for large dextrins. 2 Publications	1

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02379 Beta-D-Glucose DB04173 Fructose

DrugBankⁱ

DB02379 Beta-D-Glucose
DB04173 Fructose

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 25	Add BLAST		25
ChainⁱPRO_0000025175	26 – 446	MaltoporinAdd BLAST		421

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Disulfide bondⁱ	47 ↔ 63	1 Publication

Keywords - PTMⁱ

Disulfide bond

Proteomic databases

jPOSTⁱ	P02943
PaxDbⁱ	P02943
PRIDEⁱ	P02943

Expressionⁱ

Inductionⁱ

By maltose.

Interactionⁱ

Subunit structureⁱ

Homotrimer formed of three 18-stranded antiparallel beta-barrels, containing three independent channels.

1 Publication

Binary interactionsⁱ

P02943

With	#Exp.	IntAct
secA [P10408]	3	EBI-371309,EBI-543213

Protein-protein interaction databases

BioGridⁱ	4262663, 259 interactors
Database of interacting proteins More...DIPⁱ	DIP-10082N
IntActⁱ	P02943, 3 interactors
STRINGⁱ	511145.b4036

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	27 – 39	Combined sources	13
Beta strandⁱ	42 – 44	Combined sources	3
Beta strandⁱ	64 – 78	Combined sources	15
Beta strandⁱ	81 – 93	Combined sources	13
Beta strandⁱ	95 – 98	Combined sources	4
Beta strandⁱ	105 – 115	Combined sources	11
Beta strandⁱ	118 – 120	Combined sources	3
Beta strandⁱ	124 – 130	Combined sources	7
Beta strandⁱ	135 – 137	Combined sources	3
Helixⁱ	138 – 140	Combined sources	3
Beta strandⁱ	142 – 145	Combined sources	4
Beta strandⁱ	149 – 158	Combined sources	10
Beta strandⁱ	160 – 180	Combined sources	21
Helixⁱ	185 – 187	Combined sources	3
Beta strandⁱ	190 – 207	Combined sources	18
Beta strandⁱ	210 – 221	Combined sources	12
Beta strandⁱ	236 – 248	Combined sources	13
Beta strandⁱ	251 – 261	Combined sources	11
Helixⁱ	262 – 264	Combined sources	3
Turnⁱ	265 – 267	Combined sources	3
Beta strandⁱ	277 – 279	Combined sources	3
Beta strandⁱ	285 – 287	Combined sources	3
Beta strandⁱ	292 – 305	Combined sources	14
Turnⁱ	306 – 308	Combined sources	3
Beta strandⁱ	309 – 322	Combined sources	14
Beta strandⁱ	328 – 358	Combined sources	31
Turnⁱ	359 – 361	Combined sources	3
Beta strandⁱ	364 – 381	Combined sources	18
Beta strandⁱ	387 – 403	Combined sources	17
Turnⁱ	409 – 411	Combined sources	3
Turnⁱ	413 – 416	Combined sources	4
Beta strandⁱ	418 – 420	Combined sources	3
Helixⁱ	423 – 425	Combined sources	3
Beta strandⁱ	432 – 446	Combined sources	15

Show more details

3D structure databases

SMRⁱ	P02943
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P02943

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the porin LamB (TC 1.B.3) family. [View classification]Curated

Keywords - Domainⁱ

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGⁱ	ENOG4108KDD Bacteria COG4580 LUCA
HOGENOMⁱ	CLU_032473_4_1_6
KEGG Orthology (KO) More...KOⁱ	K02024

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01346 Maltoporin-like, 1 hit
Gene3Dⁱ	2.40.170.10, 1 hit
HAMAPⁱ	MF_01301 LamB, 1 hit
InterProⁱ	View protein in InterPro IPR023738 Maltoporin IPR003192 Porin_LamB IPR036998 Porin_LamB_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02264 LamB, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P02943-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQT 
        60         70         80         90        100
TGAQSKYRLG NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVAQQNDWE 
       110        120        130        140        150
ATDPAFREAN VQGKNLIEWL PGSTIWAGKR FYQRHDVHMI DFYYWDISGP 
       160        170        180        190        200
GAGLENIDVG FGKLSLAATR SSEAGGSSSF ASNNIYDYTN ETANDVFDVR 
       210        220        230        240        250
LAQMEINPGG TLELGVDYGR ANLRDNYRLV DGASKDGWLF TAEHTQSVLK 
       260        270        280        290        300
GFNKFVVQYA TDSMTSQGKG LSQGSGVAFD NEKFAYNINN NGHMLRILDH 
       310        320        330        340        350
GAISMGDNWD MMYVGMYQDI NWDNDNGTKW WTVGIRPMYK WTPIMSTVME 
       360        370        380        390        400
IGYDNVESQR TGDKNNQYKI TLAQQWQAGD SIWSRPAIRV FATYAKWDEK 
       410        420        430        440 
WGYDYTGNAD NNANFGKAVP ADFNGGSFGR GDSDEWTFGA QMEIWW

Length:446

Mass (Da):49,912

Last modified:July 21, 1986 - v1

Checksum:ⁱB2D4E4F120DA494E

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	35	G → GSG (PubMed:2832377).Curated	1
Sequence conflictⁱ	208	P → PDP (PubMed:2832377).Curated	1
Sequence conflictⁱ	381	S → T in AAC43130 (PubMed:8265357).Curated	1
Sequence conflictⁱ	385	R → RDP (PubMed:2832377).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M16643 Genomic DNA Translation: AAA24059.1 M26131 Genomic DNA Translation: AAA24060.1 V00298 Genomic DNA Translation: CAA23575.1 J01648 Genomic DNA Translation: AAB59058.1 U00006 Genomic DNA Translation: AAC43130.1 U00096 Genomic DNA Translation: AAC77006.1 AP009048 Genomic DNA Translation: BAE78038.1 M24997 Genomic DNA Translation: AAC41396.1 V00297 Genomic DNA Translation: CAA23574.1
PIRⁱ	A03443 QRECL
NCBI Reference Sequences More...RefSeqⁱ	NP_418460.1, NC_000913.3 WP_000973663.1, NZ_SSZK01000016.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC77006; AAC77006; b4036 BAE78038; BAE78038; BAE78038
GeneIDⁱ	948548
KEGGⁱ	ecj:JW3996 eco:b4036
PATRICⁱ	fig\|1411691.4.peg.2674

Protein	Similar proteins		Species	Score	Length	Source
P02943	Maltoporin		ECOBW		446	UniRef100_C5A130
Maltoporin		ECODH		446
Maltoporin		ECOLX		446
Maltoporin		Shigella sp.		446
Maltoporin		Salmonella sp. HNK130		446
+16

Protein	Similar proteins		Species	Score	Length	Source
P02943	Maltoporin		ECO57		446	UniRef90_Q8X5W7
Maltoporin		ECO5E		446
Maltoporin		ECO7I		446
Maltoporin		ECOSM		446
Maltoporin		ECO24		446
+528

Protein	Similar proteins		Species	Score	Length	Source
P02943	Maltoporin		KLEPN		429	UniRef50_P31242
Maltoporin 2		KLEP7		429
Maltoporin		SERP5		434
Maltoporin		YERE8		428
Maltoporin (Fragment)		YEREN		400
+2261

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M16643 Genomic DNA Translation: AAA24059.1 M26131 Genomic DNA Translation: AAA24060.1 V00298 Genomic DNA Translation: CAA23575.1 J01648 Genomic DNA Translation: AAB59058.1 U00006 Genomic DNA Translation: AAC43130.1 U00096 Genomic DNA Translation: AAC77006.1 AP009048 Genomic DNA Translation: BAE78038.1 M24997 Genomic DNA Translation: AAC41396.1 V00297 Genomic DNA Translation: CAA23574.1
PIRⁱ	A03443 QRECL
RefSeqⁱ	NP_418460.1, NC_000913.3 WP_000973663.1, NZ_SSZK01000016.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1AF6	X-ray	2.40	A/B/C	26-446	[»]
	1MAL	X-ray	3.10	A/B/C	26-446	[»]
	1MPM	X-ray	2.60	A/B/C	26-446	[»]
	1MPN	X-ray	3.20	A/B/C	26-446	[»]
	1MPO	X-ray	2.80	A/B/C	26-446	[»]
	1MPQ	X-ray	3.00	A/B/C	26-446	[»]
SMRⁱ	P02943
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262663, 259 interactors
DIPⁱ	DIP-10082N
IntActⁱ	P02943, 3 interactors
STRINGⁱ	511145.b4036

Chemistry databases

DrugBankⁱ	DB02379 Beta-D-Glucose DB04173 Fructose

DrugBankⁱ

DB02379 Beta-D-Glucose
DB04173 Fructose

Protein family/group databases

TCDBⁱ	1.B.3.1.1 the sugar porin (sp) family

TCDBⁱ

1.B.3.1.1 the sugar porin (sp) family

Proteomic databases

jPOSTⁱ	P02943
PaxDbⁱ	P02943
PRIDEⁱ	P02943

Genome annotation databases

EnsemblBacteriaⁱ	AAC77006; AAC77006; b4036 BAE78038; BAE78038; BAE78038
GeneIDⁱ	948548
KEGGⁱ	ecj:JW3996 eco:b4036
PATRICⁱ	fig\|1411691.4.peg.2674

Organism-specific databases

EchoBASEⁱ	EB0523

EchoBASEⁱ

EB0523

Phylogenomic databases

eggNOGⁱ	ENOG4108KDD Bacteria COG4580 LUCA
HOGENOMⁱ	CLU_032473_4_1_6
KOⁱ	K02024

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10528-MONOMER ECOL316407:JW3996-MONOMER MetaCyc:EG10528-MONOMER

BioCycⁱ

EcoCyc:EG10528-MONOMER
ECOL316407:JW3996-MONOMER
MetaCyc:EG10528-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P02943
Protein Ontology More...PROⁱ	PR:P02943

Family and domain databases

CDDⁱ	cd01346 Maltoporin-like, 1 hit
Gene3Dⁱ	2.40.170.10, 1 hit
HAMAPⁱ	MF_01301 LamB, 1 hit
InterProⁱ	View protein in InterPro IPR023738 Maltoporin IPR003192 Porin_LamB IPR036998 Porin_LamB_sf
Pfamⁱ	View protein in Pfam PF02264 LamB, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LAMB_ECOLI
Accessionⁱ	P02943Primary (citable) accession number: P02943 Secondary accession number(s): Q2M6R8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	April 22, 2020
	This is version 193 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

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Annotation systems

Supporting data

UniProtKB - P02943 (LAMB_ECOLI)

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Maltoporin

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P02943

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ