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Protein
Submitted name:

Extracellular lipase

Gene

lipA

Organism
Serratia marcescens
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi118Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi120Calcium 1Combined sources1
Metal bindingi144Calcium 1; via carbonyl oxygenCombined sources1
Metal bindingi153Calcium 1Combined sources1
Metal bindingi157Calcium 1Combined sources1
Metal bindingi254Calcium 2Combined sources1
Metal bindingi276Calcium 2Combined sources1
Metal bindingi284Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi285Calcium 2Combined sources1
Metal bindingi375Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi377Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi379Calcium 3Combined sources1
Metal bindingi384Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi386Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi388Calcium 4Combined sources1
Metal bindingi392Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi393Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi394Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi395Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi397Calcium 3Combined sources1
Metal bindingi397Calcium 5Combined sources1
Metal bindingi401Calcium 4Combined sources1
Metal bindingi403Calcium 4; via carbonyl oxygenCombined sources1
Metal bindingi406Calcium 4Combined sources1
Metal bindingi410Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi412Calcium 5; via carbonyl oxygenCombined sources1
Metal bindingi415Calcium 5Combined sources1
Metal bindingi491Calcium 6; via carbonyl oxygenCombined sources1
Metal bindingi493Calcium 6; via carbonyl oxygenCombined sources1
Metal bindingi495Calcium 6Combined sources1
Metal bindingi508Calcium 6; via carbonyl oxygenCombined sources1
Metal bindingi509Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi510Calcium 6; via carbonyl oxygenCombined sources1
Metal bindingi511Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi513Calcium 6Combined sources1
Metal bindingi513Calcium 7Combined sources1
Metal bindingi527Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi528Calcium 8; via carbonyl oxygenCombined sources1
Metal bindingi529Calcium 7; via carbonyl oxygenCombined sources1
Metal bindingi530Calcium 8; via carbonyl oxygenCombined sources1
Metal bindingi532Calcium 7Combined sources1
Metal bindingi532Calcium 8Combined sources1
Metal bindingi549Calcium 8; via carbonyl oxygenCombined sources1
Metal bindingi552Calcium 8Combined sources1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Protein family/group databases

ESTHERiserma-lipasA. Bacterial_lip_FamI.3.

Names & Taxonomyi

Protein namesi
Submitted name:
Extracellular lipaseImported (EC:3.1.1.3Imported)
Gene namesi
Name:lipAImported
OrganismiSerratia marcescensImported
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QUAX-ray1.95A1-613[»]
2QUBX-ray1.80A/C/E/G/I/K1-613[»]
ProteinModelPortaliQ59933.
SMRiQ59933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59933.

Family & Domainsi

Family and domain databases

Gene3Di2.150.10.10. 2 hits.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 2 hits.
SSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59933-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIFSYKDLD ENASKALFSD ALAISTYAYH NIDNGFDEGY HQTGFGLGLP
60 70 80 90 100
LTLITALIGS TQSQGGLPGL PWNPDSEQAA QEAVNNAGWS VISATQLGYA
110 120 130 140 150
GKTDARGTYY GETAGYTTAQ AEVLGKYDSE GNLTAIGISF RGTSGPRESL
160 170 180 190 200
IGDTIGDVIN DLLAGFGPKG YADGYTLKAF GNLLGDVAKF AQAHGLSGED
210 220 230 240 250
VVVSGHSLGG LAVNSMAAQS DANWGGFYAQ SNYVAFASPT QYEAGGKVIN
260 270 280 290 300
IGYENDPVFR ALDGTSLTLP SLGVHDAPHT SATNNIVNFN DHYASDAWNL
310 320 330 340 350
LPFSILNIPT WLSHLPFFYQ DGLMRVLNSE FYSLTDKDST IIVSNLSNVT
360 370 380 390 400
RGNTWVEDLN RNAETHSGPT FIIGSDGNDL IKGGKGNDYL EGRDGDDIFR
410 420 430 440 450
DAGGYNLIAG GKGHNIFDTQ QALKNTEVAY DGNTLYLRDA KGGITLADDI
460 470 480 490 500
STLRSKETSW LIFNKEVDHQ VTAAGLKSDS GLKAYAAATG GDGDDVLQAR
510 520 530 540 550
SHDAWLFGNA GNDTLIGHAG GNLTFVGGSG DDILKGVGNG NTFLFSGDFG
560 570 580 590 600
RDQLYGFNAS DKLVFIGTEG ASGNIRDYAT QQNDDLVLAF GHSQVTLIGV
610
SLDHISTDQV VLA
Length:613
Mass (Da):64,798
Last modified:November 1, 1996 - v1
Checksum:i64A108A5AB52BB76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11258 Genomic DNA. Translation: AAA81002.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11258 Genomic DNA. Translation: AAA81002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QUAX-ray1.95A1-613[»]
2QUBX-ray1.80A/C/E/G/I/K1-613[»]
ProteinModelPortaliQ59933.
SMRiQ59933.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiserma-lipasA. Bacterial_lip_FamI.3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ59933.

Family and domain databases

Gene3Di2.150.10.10. 2 hits.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
SUPFAMiSSF51120. SSF51120. 2 hits.
SSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ59933_SERMA
AccessioniPrimary (citable) accession number: Q59933
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.