UniProtKB - Q9X7U2 (CHPB_STRCO)
Protein
Chaplin-B
Gene
chpB
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Functioni
One of 8 partially redundant surface-active proteins required for efficient formation of aerial mycelium; the short chaplins assemble into a hydrophobic, amyloidal fibrillar surface layer that envelopes and protects aerial hyphae and spores, presumably anchored to the long chaplins (PubMed:12832396, PubMed:12832397, PubMed:15228525, PubMed:17462011). Chaplins have an overlapping function with the surface-active SapB peptide; chaplins are essential on minimal medium while on rich medium both chaplins and SapB are required for efficient aerial hyphae formation (PubMed:17462011). The long chaplins (ChpA, ChpB, ChpC) are not absolutely necessary for short chaplin localization or rodlet formation, but probably play a role in initiating aerial hyphae development (PubMed:22296345). Chaplins are also involved in cell attachment to a hydrophobic surface (PubMed:19682261).6 Publications
GO - Biological processi
- cell adhesion Source: UniProtKB-KW
Keywordsi
Biological process | Cell adhesion |
Names & Taxonomyi
Protein namesi | Recommended name: Chaplin-B1 Publication |
Gene namesi | Name:chpB1 Publication Ordered Locus Names:SCO7257 |
Organismi | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
Taxonomic identifieri | 100226 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Streptomycetales › Streptomycetaceae › Streptomyces › Streptomyces albidoflavus group › |
Proteomesi |
|
Subcellular locationi
Cell wall
- cell wall PROSITE-ProRule annotation2 Publications; Peptidoglycan-anchor PROSITE-ProRule annotation2 Publications
Note: Anchored to the cell wall by at least one of sortases SrtE1 and SrtE2.1 Publication
Cell Wall
- cell wall Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular region Source: UniProtKB-KW
Keywords - Cellular componenti
Amyloid, Cell wall, SecretedPathology & Biotechi
Disruption phenotypei
A single chpB disruption has no phenotype; a quadruple chpA-chpC-chpD-chpH knockout has delayed aerial hyphae formation and sporulation. A quintuple chpA-chpB-chpC-chpD-chpH knockout has a longer delay in aerial hyphae formation and an almost complete lack of sporulation. The quintuple knockout still expresses ChpE, ChpF and ChpG (PubMed:12832397). Quintuple knockout chpA-chpB-chpC-chpD-chpH has strongly delayed aerial hyphae formation, makes many fewer aerial hyphae but no effect on viability of the spores produced. Further deletion of chpE leads to more severe effects, and on rich media few aerial hyphae are produced after prolonged growth. Those few hyphae do differentiate into spores and have a rodlet layer (PubMed:12832396). Deletion of all 8 chaplin genes on minimal medium leads to severely disrupted aerial hyphae that collapse on the colony surface and are not hydrophobic. A few spore chains can still be made, but they have neither rodlets or amyloid-like fibers. rdlA and rdlB mRNA are down-regulated (PubMed:15228525, PubMed:17462011). Deletion of all 8 chaplin genes on rich medium leads to a reduced abundance of aerial hyphae without rodlets and occasional spore chains on surface hyphae. A complete chaplin-negative plus ram-negative strain (deletion of ramR or the ramC-ramS-ramA-ramB operon) leads to the complete loss of robust aerial hyphae (PubMed:17462011). Deletion of the 3 long chaplins (ChpA, ChpB, ChpC) results in a 24 hour delay in aerial hyphae formation, while rodlets are about 1.5-fold longer than wild-type (PubMed:22296345). Deletion of all 8 chaplin genes significantly reduces cellular attachment to a hydrophobic substrate; thin fibrils instead of fimbrae are detected. The long chaplins (ChpA, ChpB and ChpC, as seen by near wild-type attachment of the hextuple chpA-chpB-chpC-chpD-chpE-chpH knockout) are not essential but may contribute to cellular attachment (PubMed:19682261).6 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 26 | Sequence analysisAdd BLAST | 26 | |
ChainiPRO_5004336275 | 27 – 237 | Chaplin-BSequence analysisAdd BLAST | 211 | |
PropeptideiPRO_0000445189 | 206 – 237 | Removed by sortasePROSITE-ProRule annotationAdd BLAST | 32 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 205 | Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Peptidoglycan-anchorExpressioni
Inductioni
Transcribed during aerial hyphae formation on minimal medium, about 10- to 25-fold lower expression than the short chaplins. Weak expression in aerial hyphae (at protein level) (Probable). Very low expression on rich medium, unaffected by ECF sigma factor BldN (PubMed:12832397).1 Publication1 Publication
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 42 – 82 | Chaplin 1PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 120 – 160 | Chaplin 2PROSITE-ProRule annotationAdd BLAST | 41 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 202 – 206 | LPXTG sorting signalPROSITE-ProRule annotation | 5 |
Sequence similaritiesi
Keywords - Domaini
Repeat, SignalPhylogenomic databases
eggNOGi | ENOG5034C0V, Bacteria |
HOGENOMi | CLU_070271_0_0_11 |
OMAi | GNACANT |
Family and domain databases
InterProi | View protein in InterPro IPR005528, ChpA-H IPR019931, LPXTG_anchor |
Pfami | View protein in Pfam PF03777, ChpA-C, 2 hits |
PROSITEi | View protein in PROSITE PS51884, CHAPLIN, 2 hits PS50847, GRAM_POS_ANCHORING, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9X7U2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRRVTRNGVL AVAASGALAV TMPAYAAFAS DGAGAEGSAA GSPGLISGNT
60 70 80 90 100
VQLPVDVPVD VCGNTVNVVG LLNPAAGNGC ADSGEPGASY QAAGASGGTS
110 120 130 140 150
GSATEATSGG AAAEGSGKDS PGVLSGNGVQ LPVHLPVNVS GNSVNVVGIG
160 170 180 190 200
NPAVGNESTN DSGDHPEPVR PPAEPEPSAP EEERAGPGPS AHAAPPREEV
210 220 230
SLAHTGTDRT LPTLAGGAAL VLGGTVLYRR FRPGSGD
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL939131 Genomic DNA Translation: CAB42960.1 |
PIRi | T35351 |
RefSeqi | NP_631313.1, NC_003888.3 WP_011031547.1, NC_003888.3 |
Genome annotation databases
GeneIDi | 1102695 |
KEGGi | sco:SCO7257 |
PATRICi | fig|100226.15.peg.7359 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL939131 Genomic DNA Translation: CAB42960.1 |
PIRi | T35351 |
RefSeqi | NP_631313.1, NC_003888.3 WP_011031547.1, NC_003888.3 |
3D structure databases
SMRi | Q9X7U2 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 100226.SCO7257 |
Genome annotation databases
GeneIDi | 1102695 |
KEGGi | sco:SCO7257 |
PATRICi | fig|100226.15.peg.7359 |
Phylogenomic databases
eggNOGi | ENOG5034C0V, Bacteria |
HOGENOMi | CLU_070271_0_0_11 |
OMAi | GNACANT |
Family and domain databases
InterProi | View protein in InterPro IPR005528, ChpA-H IPR019931, LPXTG_anchor |
Pfami | View protein in Pfam PF03777, ChpA-C, 2 hits |
PROSITEi | View protein in PROSITE PS51884, CHAPLIN, 2 hits PS50847, GRAM_POS_ANCHORING, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CHPB_STRCO | |
Accessioni | Q9X7U2Primary (citable) accession number: Q9X7U2 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 10, 2018 |
Last sequence update: | November 1, 1999 | |
Last modified: | April 7, 2021 | |
This is version 86 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
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families