UniProtKB - P0A940 (BAMA_ECOLI)
Protein
Outer membrane protein assembly factor BamA
Gene
bamA
Organism
Escherichia coli (strain K12)
Status
Functioni
Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).9 Publications
(Microbial infection) Acts as a receptor for CdiA-EC93, the contact-dependent growth inhibition (CDI) effector of E.coli strain EC93; antibodies against extracellular epitopes decrease CDI. Its role in CDI is independent of the other Bam complex components (PubMed:18761695). Is not the receptor for CdiA from E.coli strain 536 / UPEC, which does not have the same mode of toxicity as CdiA from strain EC93; the decreased expression of bamA101 in some experiments decreases the level of outer membrane proteins in general (PubMed:23469034, PubMed:23882017). Susceptibility to CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders cells resistant to CdiA-EC93. Cells with BamA from another bacteria no longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in which E.cloacae extracellular loops 6 and 7 are replaced with loops 6 and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from strain 536 / UPEC (PubMed:23882017).3 Publications
GO - Biological processi
- cell adhesion Source: UniProtKB-KW
- Gram-negative-bacterium-type cell outer membrane assembly Source: EcoCyc
- protein insertion into membrane Source: EcoCyc
Keywordsi
Biological process | Cell adhesion |
Enzyme and pathway databases
BioCyci | EcoCyc:G6093-MONOMER |
Names & Taxonomyi
Protein namesi | Recommended name: Outer membrane protein assembly factor BamAUniRule annotationAlternative name(s): Omp85 |
Gene namesi | Name:bamAUniRule annotation Synonyms:yaeT, yzzN, yzzY Ordered Locus Names:b0177, JW0172 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell outer membrane UniRule annotation6 Publications
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 21 – 424 | PeriplasmicCuratedAdd BLAST | 404 | |
Transmembranei | 425 – 433 | Beta stranded; Name=Strand 11 Publication | 9 | |
Topological domaini | 434 – 435 | Extracellular; loop 1Curated | 2 | |
Transmembranei | 436 – 446 | Beta stranded; Name=Strand 21 PublicationAdd BLAST | 11 | |
Topological domaini | 447 – 454 | PeriplasmicCurated | 8 | |
Transmembranei | 455 – 462 | Beta stranded; Name=Strand 31 Publication | 8 | |
Topological domaini | 463 – 465 | Extracellular; loop 2Curated | 3 | |
Transmembranei | 466 – 475 | Beta stranded; Name=Strand 41 Publication | 10 | |
Topological domaini | 476 – 483 | PeriplasmicCurated | 8 | |
Transmembranei | 484 – 495 | Beta stranded; Name=Strand 51 PublicationAdd BLAST | 12 | |
Topological domaini | 496 – 504 | Extracellular; loop 3Curated | 9 | |
Transmembranei | 505 – 506 | Beta stranded; Name=Strand 61 Publication | 2 | |
Topological domaini | 507 – 522 | PeriplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 523 – 535 | Beta stranded; Name=Strand 71 PublicationAdd BLAST | 13 | |
Topological domaini | 536 – 563 | Extracellular; loop 42 PublicationsAdd BLAST | 28 | |
Transmembranei | 564 – 577 | Beta stranded; Name=Strand 81 PublicationAdd BLAST | 14 | |
Topological domaini | 578 – 590 | PeriplasmicCuratedAdd BLAST | 13 | |
Transmembranei | 591 – 600 | Beta stranded; Name=Strand 91 Publication | 10 | |
Topological domaini | 601 – 608 | Extracellular; loop 5Curated | 8 | |
Transmembranei | 609 – 619 | Beta stranded; Name=Strand 101 PublicationAdd BLAST | 11 | |
Topological domaini | 620 – 628 | PeriplasmicCurated | 9 | |
Transmembranei | 629 – 639 | Beta stranded; Name=Strand 111 PublicationAdd BLAST | 11 | |
Topological domaini | 640 – 708 | Extracellular; loop 62 PublicationsAdd BLAST | 69 | |
Transmembranei | 709 – 718 | Beta stranded; Name=Strand 121 Publication | 10 | |
Topological domaini | 719 – 732 | PeriplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 733 – 745 | Beta stranded; Name=Strand 131 PublicationAdd BLAST | 13 | |
Topological domaini | 746 – 767 | Extracellular; loop 7CuratedAdd BLAST | 22 | |
Transmembranei | 768 – 777 | Beta stranded; Name=Strand 141 Publication | 10 | |
Topological domaini | 778 | PeriplasmicCurated | 1 | |
Transmembranei | 779 – 789 | Beta stranded; Name=Strand 151 PublicationAdd BLAST | 11 | |
Topological domaini | 790 – 803 | Extracellular; loop 8CuratedAdd BLAST | 14 | |
Transmembranei | 804 – 808 | Beta stranded; Name=Strand 161 Publication | 5 |
GO - Cellular componenti
- Bam protein complex Source: EcoCyc
- cell outer membrane Source: EcoCyc
- integral component of membrane Source: UniProtKB-KW
Keywords - Cellular componenti
Cell outer membrane, MembranePathology & Biotechi
Disruption phenotypei
Deletion is lethal. Depletion results in the accumulation of incorrectly assembled outer membrane proteins, including TolC, OmpF, OmpC and OmpA (PubMed:15851030, PubMed:16102012). Decreased expression leads to decreased susceptibility to contact-dependent growth inhibition (CDI), and decreased expression of outer membrane proteins (including in this study LamB) as well as up-regulation of periplasmic protease DegP (PubMed:18761695, PubMed:23469034).4 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 181 | N → A: Lethal, protein does not accumulate. 1 Publication | 1 | |
Mutagenesisi | 251 | K → A: Lethal, protein does not accumulate. 1 Publication | 1 | |
Mutagenesisi | 259 | N → A: Lethal, protein does not accumulate. 1 Publication | 1 | |
Mutagenesisi | 351 – 353 | KIR → PIP: Lethal, wild-type protein levels. 1 Publication | 3 | |
Mutagenesisi | 351 | K → P: Reduces cell growth, wild-type protein levels. 1 Publication | 1 | |
Mutagenesisi | 366 | R → E: Severely impairs cell growth, wild-type protein levels. 1 Publication | 1 | |
Mutagenesisi | 373 | E → K: Lethal, wild-type protein levels. 2 Publications | 1 | |
Mutagenesisi | 393 | G → C: No effect. Lethal; when associated with C-584, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication | 1 | |
Mutagenesisi | 415 – 419 | VYKVK → PYKVP: Lethal, wild-type protein levels. 1 Publication | 5 | |
Mutagenesisi | 415 – 417 | VYK → PYP: Lethal, wild-type protein levels. 1 Publication | 3 | |
Mutagenesisi | 417 – 419 | KVK → PVP: Lethal, wild-type protein levels. 1 Publication | 3 | |
Mutagenesisi | 429 | G → P: Lethal, wild-type protein levels. 1 Publication | 1 | |
Mutagenesisi | 430 | I → C: Reduced folding of OmpT; when associated with C-808, traps protein in lateral closed conformation, growth restored by reducing agent. 1 Publication | 1 | |
Mutagenesisi | 435 | E → C: No effect. Lethal; when associated with C-658 or C-665, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication | 1 | |
Mutagenesisi | 435 | E → L: Very minor growth defect. Lethal; when associated with L-800. 1 Publication | 1 | |
Mutagenesisi | 464 | D → L: Very minor growth defect. 1 Publication | 1 | |
Mutagenesisi | 500 | D → L: Very minor growth defect. 1 Publication | 1 | |
Mutagenesisi | 547 | R → A: Lethal. 1 Publication | 1 | |
Mutagenesisi | 554 – 562 | EHPSTSDQD → VDYPYDVPDYA: Loop 4 to HA epitope; still susceptible to CdiA-EC93. 1 Publication | 9 | |
Mutagenesisi | 556 – 563 | PSTSDQDN → G: Delta loop 4; slight increase in resistance to CdiA-EC93, forms aggregates with CdiA-EC93 cells. 1 Publication | 8 | |
Mutagenesisi | 584 | G → C: No effect. Lethal; when associated with C-393, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication | 1 | |
Mutagenesisi | 658 | S → C: No effect. Lethal; when associated with C-435, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication | 1 | |
Mutagenesisi | 661 | R → A: Slow growth on solid and liquid media, less protein accumulates which is more proteinase sensitive. 1 Publication | 1 | |
Mutagenesisi | 665 | S → C: No effect. Lethal; when associated with C-435, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication | 1 | |
Mutagenesisi | 673 – 702 | Missing : Lethal. 1 PublicationAdd BLAST | 30 | |
Mutagenesisi | 675 – 701 | FPHQA…KDLCK → G: Delta loop 6; fully resistant to CdiA-EC93, does not form aggregates with CdiA-EC93 cells. 1 PublicationAdd BLAST | 27 | |
Mutagenesisi | 677 – 685 | HQASNYDPD → VDYPYDVPDYA: Loop 6 to HA epitope; still susceptible to CdiA-EC93. 1 Publication | 9 | |
Mutagenesisi | 740 | D → A: Slow growth on solid and liquid media, less protein accumulates which is more proteinase sensitive. 1 Publication | 1 | |
Mutagenesisi | 754 – 755 | YS → VDYPYDVPDYA: Loop 7 to HA epitope; fully resistant to CdiA-EC93, does not form aggregates with CdiA-EC93 cells. 1 Publication | 2 | |
Mutagenesisi | 800 | E → L: Very minor growth defect. Lethal; when associated with L-435. 1 Publication | 1 | |
Mutagenesisi | 808 | K → C: Reduced folding of OmpT; when associated with C-430, traps protein in lateral closed conformation, growth restored by reducing agent. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | UniRule annotation1 PublicationAdd BLAST | 20 | |
ChainiPRO_0000033470 | 21 – 810 | Outer membrane protein assembly factor BamAAdd BLAST | 790 |
Proteomic databases
jPOSTi | P0A940 |
PaxDbi | P0A940 |
PRIDEi | P0A940 |
2D gel databases
SWISS-2DPAGEi | P0A940 |
PTM databases
CarbonylDBi | P0A940 |
Interactioni
Subunit structurei
Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. BamA interacts directly with BamB and the BamCDE subcomplex. The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).
10 PublicationsBinary interactionsi
Hide detailsP0A940
With | #Exp. | IntAct |
---|---|---|
bamB [P77774] | 23 | EBI-907371,EBI-907297 |
bamD [P0AC02] | 26 | EBI-907371,EBI-1128087 |
rcsF [P69411] | 3 | EBI-907371,EBI-1114706 |
Protein-protein interaction databases
BioGRIDi | 4259504, 747 interactors |
ComplexPortali | CPX-1923, BAM complex |
DIPi | DIP-36019N |
IntActi | P0A940, 14 interactors |
STRINGi | 511145.b0177 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A940 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A940 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 24 – 91 | POTRA 1PROSITE-ProRule annotation1 PublicationAdd BLAST | 68 | |
Domaini | 92 – 172 | POTRA 2PROSITE-ProRule annotation1 PublicationAdd BLAST | 81 | |
Domaini | 175 – 263 | POTRA 3PROSITE-ProRule annotation1 PublicationAdd BLAST | 89 | |
Domaini | 266 – 344 | POTRA 4PROSITE-ProRule annotation1 PublicationAdd BLAST | 79 | |
Domaini | 347 – 421 | POTRA 5PROSITE-ProRule annotation1 PublicationAdd BLAST | 75 |
Domaini
Contains 5 N-terminal periplasmic polypeptide transport-associated (POTRA) domains which interact with other subunits of the complex, may recruit substrates from the periplasm into the outer membrane and also act as a chaperone (PubMed:17702946, PubMed:18430136, PubMed:19081063, PubMed:21795783, PubMed:14559180). The C-terminal region forms a discontinuous 16-stranded beta-barrel transmembrane region. The central pore is ellipsoid, and probably closed by extracellular loop 6, perhaps with the aid of other loops (PubMed:24914988, PubMed:24619089).1 Publication6 Publications
Sequence similaritiesi
Belongs to the BamA family.UniRule annotation
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane beta strandPhylogenomic databases
eggNOGi | COG4775, Bacteria |
HOGENOMi | CLU_007664_1_0_6 |
InParanoidi | P0A940 |
PhylomeDBi | P0A940 |
Family and domain databases
HAMAPi | MF_01430, OM_assembly_BamA, 1 hit |
InterProi | View protein in InterPro IPR000184, Bac_surfAg_D15 IPR010827, BamA/TamA_POTRA IPR039910, D15-like IPR023707, OM_assembly_BamA IPR034746, POTRA |
PANTHERi | PTHR12815, PTHR12815, 1 hit PTHR12815:SF23, PTHR12815:SF23, 1 hit |
Pfami | View protein in Pfam PF01103, Omp85, 1 hit PF07244, POTRA, 4 hits |
PIRSFi | PIRSF006076, OM_assembly_OMP85, 1 hit |
TIGRFAMsi | TIGR03303, OM_YaeT, 1 hit |
PROSITEi | View protein in PROSITE PS51779, POTRA, 5 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A940-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT
60 70 80 90 100
GDTVNDEDIS NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS
110 120 130 140 150
GNKSVKDDML KQNLEASGVR VGESLDRTTI ADIEKGLEDF YYSVGKYSAS
160 170 180 190 200
VKAVVTPLPR NRVDLKLVFQ EGVSAEIQQI NIVGNHAFTT DELISHFQLR
210 220 230 240 250
DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI DSTQVSLTPD
260 270 280 290 300
KKGIYVTVNI TEGDQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK
310 320 330 340 350
VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDAGNRFYVR
360 370 380 390 400
KIRFEGNDTS KDAVLRREMR QMEGAWLGSD LVDQGKERLN RLGFFETVDT
410 420 430 440 450
DTQRVPGSPD QVDVVYKVKE RNTGSFNFGI GYGTESGVSF QAGVQQDNWL
460 470 480 490 500
GTGYAVGING TKNDYQTYAE LSVTNPYFTV DGVSLGGRLF YNDFQADDAD
510 520 530 540 550
LSDYTNKSYG TDVTLGFPIN EYNSLRAGLG YVHNSLSNMQ PQVAMWRYLY
560 570 580 590 600
SMGEHPSTSD QDNSFKTDDF TFNYGWTYNK LDRGYFPTDG SRVNLTGKVT
610 620 630 640 650
IPGSDNEYYK VTLDTATYVP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE
660 670 680 690 700
NFYAGGSSTV RGFQSNTIGP KAVYFPHQAS NYDPDYDYEC ATQDGAKDLC
710 720 730 740 750
KSDDAVGGNA MAVASLEFIT PTPFISDKYA NSVRTSFFWD MGTVWDTNWD
760 770 780 790 800
SSQYSGYPDY SDPSNIRMSA GIALQWMSPL GPLVFSYAQP FKKYDGDKAE
810
QFQFNIGKTW
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 115 | E → Q in AAK64508 (Ref. 2) Curated | 1 | |
Sequence conflicti | 228 | S → I in AAK64508 (Ref. 2) Curated | 1 | |
Sequence conflicti | 361 | K → R in AAK64508 (Ref. 2) Curated | 1 | |
Sequence conflicti | 632 | R → C in AAK64508 (Ref. 2) Curated | 1 | |
Sequence conflicti | 712 | A → T in AAK64508 (Ref. 2) Curated | 1 |
Mass spectrometryi
Molecular mass is 88426 Da. Determined by ESI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF407013 Genomic DNA Translation: AAL01379.1 AY035865 Genomic DNA Translation: AAK64508.1 U70214 Genomic DNA Translation: AAB08606.1 U00096 Genomic DNA Translation: AAC73288.1 AP009048 Genomic DNA Translation: BAA77852.2 |
PIRi | A64742 |
RefSeqi | NP_414719.1, NC_000913.3 WP_001240896.1, NZ_STEB01000032.1 |
Genome annotation databases
EnsemblBacteriai | AAC73288; AAC73288; b0177 BAA77852; BAA77852; BAA77852 |
GeneIDi | 57731438 944870 |
KEGGi | ecj:JW0172 eco:b0177 |
PATRICi | fig|1411691.4.peg.2102 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF407013 Genomic DNA Translation: AAL01379.1 AY035865 Genomic DNA Translation: AAK64508.1 U70214 Genomic DNA Translation: AAB08606.1 U00096 Genomic DNA Translation: AAC73288.1 AP009048 Genomic DNA Translation: BAA77852.2 |
PIRi | A64742 |
RefSeqi | NP_414719.1, NC_000913.3 WP_001240896.1, NZ_STEB01000032.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2QCZ | X-ray | 2.70 | A/B | 21-351 | [»] | |
2QDF | X-ray | 2.20 | A | 21-351 | [»] | |
2V9H | NMR | - | A | 21-184 | [»] | |
3EFC | X-ray | 3.30 | A | 21-410 | [»] | |
3OG5 | X-ray | 2.69 | A/B | 264-424 | [»] | |
3Q6B | X-ray | 1.50 | A | 266-420 | [»] | |
4C4V | X-ray | 3.00 | A | 347-810 | [»] | |
B | 344-810 | [»] | ||||
4N75 | X-ray | 2.60 | A/B | 427-810 | [»] | |
4PK1 | X-ray | 3.10 | A | 175-424 | [»] | |
4XGA | X-ray | 2.15 | B | 175-420 | [»] | |
5AYW | X-ray | 3.56 | A | 22-810 | [»] | |
5D0O | X-ray | 2.90 | A | 1-810 | [»] | |
5D0Q | X-ray | 3.50 | A/F | 1-810 | [»] | |
5EKQ | X-ray | 3.39 | A | 21-810 | [»] | |
5LJO | electron microscopy | 4.90 | A | 24-806 | [»] | |
6SN9 | electron microscopy | 9.80 | A | 24-806 | [»] | |
6T1W | X-ray | 3.79 | A/B | 1-810 | [»] | |
6V05 | electron microscopy | 4.10 | A | 1-810 | [»] | |
F | 1-810 | [»] | ||||
SMRi | P0A940 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259504, 747 interactors |
ComplexPortali | CPX-1923, BAM complex |
DIPi | DIP-36019N |
IntActi | P0A940, 14 interactors |
STRINGi | 511145.b0177 |
PTM databases
CarbonylDBi | P0A940 |
2D gel databases
SWISS-2DPAGEi | P0A940 |
Proteomic databases
jPOSTi | P0A940 |
PaxDbi | P0A940 |
PRIDEi | P0A940 |
Genome annotation databases
EnsemblBacteriai | AAC73288; AAC73288; b0177 BAA77852; BAA77852; BAA77852 |
GeneIDi | 57731438 944870 |
KEGGi | ecj:JW0172 eco:b0177 |
PATRICi | fig|1411691.4.peg.2102 |
Organism-specific databases
EchoBASEi | EB2541 |
Phylogenomic databases
eggNOGi | COG4775, Bacteria |
HOGENOMi | CLU_007664_1_0_6 |
InParanoidi | P0A940 |
PhylomeDBi | P0A940 |
Enzyme and pathway databases
BioCyci | EcoCyc:G6093-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0A940 |
PROi | PR:P0A940 |
Family and domain databases
HAMAPi | MF_01430, OM_assembly_BamA, 1 hit |
InterProi | View protein in InterPro IPR000184, Bac_surfAg_D15 IPR010827, BamA/TamA_POTRA IPR039910, D15-like IPR023707, OM_assembly_BamA IPR034746, POTRA |
PANTHERi | PTHR12815, PTHR12815, 1 hit PTHR12815:SF23, PTHR12815:SF23, 1 hit |
Pfami | View protein in Pfam PF01103, Omp85, 1 hit PF07244, POTRA, 4 hits |
PIRSFi | PIRSF006076, OM_assembly_OMP85, 1 hit |
TIGRFAMsi | TIGR03303, OM_YaeT, 1 hit |
PROSITEi | View protein in PROSITE PS51779, POTRA, 5 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BAMA_ECOLI | |
Accessioni | P0A940Primary (citable) accession number: P0A940 Secondary accession number(s): P39170 Q9R2E3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 19, 2005 |
Last sequence update: | July 19, 2005 | |
Last modified: | February 10, 2021 | |
This is version 139 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families