COMP_ACIAD
ID COMP_ACIAD Reviewed; 147 AA.
AC O30583; Q6F7F8;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Pilin-like competence factor ComP {ECO:0000303|PubMed:10850981};
DE Flags: Precursor;
GN Name=comP {ECO:0000303|PubMed:9361398};
GN OrderedLocusNames=ACIAD3338 {ECO:0000312|EMBL:CAG70007.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=9361398; DOI=10.1128/aem.63.11.4150-4157.1997;
RA Porstendorfer D., Drotschmann U., Averhoff B.;
RT "A novel competence gene, comP, is essential for natural transformation of
RT Acinetobacter sp. strain BD413.";
RL Appl. Environ. Microbiol. 63:4150-4157(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3]
RP FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=10850981; DOI=10.1128/jb.182.13.3673-3680.2000;
RA Porstendoerfer D., Gohl O., Mayer F., Averhoff B.;
RT "ComP, a pilin-like protein essential for natural competence in
RT Acinetobacter sp. strain BD413: regulation, modification, and cellular
RT localization.";
RL J. Bacteriol. 182:3673-3680(2000).
RN [4]
RP GLYCOSYLATION.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=23658772; DOI=10.1371/journal.pone.0062768;
RA Schulz B.L., Jen F.E., Power P.M., Jones C.E., Fox K.L., Ku S.C.,
RA Blanchfield J.T., Jennings M.P.;
RT "Identification of bacterial protein O-oligosaccharyltransferases and their
RT glycoprotein substrates.";
RL PLoS ONE 8:E62768-E62768(2013).
CC -!- FUNCTION: Pilin-like competence factor, which is essential for natural
CC transformation of the Gram-negative soil bacterium A.baylyi ADP1. Is
CC not a subunit of the pilus structures. Likely functions as a major
CC subunit of an oligomeric structure acting as a channel or pore
CC mediating DNA translocation through the outer membrane and periplasm.
CC {ECO:0000269|PubMed:10850981, ECO:0000269|PubMed:9361398}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:10850981}. Periplasm {ECO:0000269|PubMed:10850981}.
CC Cell outer membrane {ECO:0000269|PubMed:10850981}. Note=The 20-kDa form
CC is present in the cytoplasmic membrane, the periplasm, and the outer
CC membrane, whereas the 23-kDa form is located in the outer membrane and
CC might be due to a further modification. {ECO:0000269|PubMed:10850981}.
CC -!- INDUCTION: Is maximally expressed in the late stationary growth phase
CC (at protein and mRNA level). Minimal comP expression levels are
CC detected in the middle of the logarithmic growth phase.
CC {ECO:0000269|PubMed:10850981}.
CC -!- PTM: Glycosylated by PglL2 (PubMed:23658772). The 20-kDa form is
CC glycosylated; a 23-kDa form also exists, that might be due to a further
CC modification. The glycosylation of ComP is not required for its
CC function in DNA binding and uptake (PubMed:10850981).
CC {ECO:0000269|PubMed:10850981, ECO:0000269|PubMed:23658772}.
CC -!- DISRUPTION PHENOTYPE: A deletion of comP completely abolishes natural
CC transformation, due to a complete lack of DNA binding and, therefore,
CC uptake of DNA, but has no effect on piliation and on twitching
CC motility. {ECO:0000269|PubMed:9361398}.
CC -!- SIMILARITY: Belongs to the N-Me-Phe pilin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF012550; AAC45886.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG70007.1; -; Genomic_DNA.
DR RefSeq; WP_004923779.1; NC_005966.1.
DR AlphaFoldDB; O30583; -.
DR SMR; O30583; -.
DR STRING; 62977.ACIAD3338; -.
DR EnsemblBacteria; CAG70007; CAG70007; ACIAD3338.
DR GeneID; 45235535; -.
DR KEGG; aci:ACIAD3338; -.
DR eggNOG; COG4969; Bacteria.
DR HOGENOM; CLU_091705_4_0_6; -.
DR OMA; ATAHCAI; -.
DR OrthoDB; 1970253at2; -.
DR BioCyc; ASP62977:ACIAD_RS15100-MON; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR InterPro; IPR012902; N_methyl_site.
DR InterPro; IPR001082; Pilin.
DR InterPro; IPR045584; Pilin-like.
DR Pfam; PF07963; N_methyl; 1.
DR Pfam; PF00114; Pilin; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
DR TIGRFAMs; TIGR02532; IV_pilin_GFxxxE; 1.
DR PROSITE; PS00409; PROKAR_NTER_METHYL; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cell outer membrane; Competence;
KW DNA-binding; Glycoprotein; Membrane; Methylation; Periplasm;
KW Reference proteome.
FT PROPEP 1..6
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
FT /id="PRO_0000433788"
FT CHAIN 7..147
FT /note="Pilin-like competence factor ComP"
FT /id="PRO_0000433789"
FT MOD_RES 7
FT /note="N-methylphenylalanine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01070"
SQ SEQUENCE 147 AA; 14872 MW; 682DBC062230C479 CRC64;
MNAQKGFTLI ELMIVIAIIG ILAAIAIPAY TDYTVRARVS EGLTAASSMK TTVSENILNA
GALVAGTPST AGSSCVGVQE ISASNATTNV ATATCGASSA GQIIVTMDTT KAKGANITLT
PTYASGAVTW KCTTTSDKKY VPSECRG
