ASA1_ENTFA
ID ASA1_ENTFA Reviewed; 1296 AA.
AC P17953;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Aggregation substance;
DE Flags: Precursor;
GN Name=asa1; OrderedLocusNames=EF_A0047;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OG Plasmid pTEF1, and Plasmid pAD1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 44-51.
RC STRAIN=DS16; PLASMID=pAD1;
RX PubMed=2120541; DOI=10.1111/j.1365-2958.1990.tb00662.x;
RA Galli D., Lottspeich F., Wirth R.;
RT "Sequence analysis of Enterococcus faecalis aggregation substance encoded
RT by the sex pheromone plasmid pAD1.";
RL Mol. Microbiol. 4:895-904(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583; PLASMID=pTEF1;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Aggregation substance allows donor and recipient strains to
CC form tight aggregates which allow the non-motile bacteria to maintain
CC physical contact over a period of time sufficient to permit conjugative
CC transfer of the sex pheromone plasmid from donor to recipient strains.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- SIMILARITY: Belongs to the antigen I/II family. {ECO:0000305}.
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DR EMBL; X17214; CAA35083.1; -; Genomic_DNA.
DR EMBL; AE016833; AAO83043.1; -; Genomic_DNA.
DR PIR; S10223; HMSO1F.
DR RefSeq; NP_816972.1; NC_004669.1.
DR RefSeq; WP_010785625.1; NZ_KE136530.1.
DR AlphaFoldDB; P17953; -.
DR SMR; P17953; -.
DR EnsemblBacteria; AAO83043; AAO83043; EF_A0047.
DR KEGG; efa:EFA0047; -.
DR PATRIC; fig|226185.46.peg.3217; -.
DR HOGENOM; CLU_007908_0_0_9; -.
DR Proteomes; UP000001415; Plasmid pTEF1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 2.60.530.10; -; 1.
DR InterPro; IPR026345; Adh_isopep-form_adh_dom.
DR InterPro; IPR041324; AgI/II_N.
DR InterPro; IPR032300; Antigen_C.
DR InterPro; IPR013574; Glucan-bd_C/Surface_Ag-I/II_V.
DR InterPro; IPR022263; KxYKxGKxW.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR036234; SA_I/II_PAC_V_sf.
DR Pfam; PF18652; Adhesin_P1_N; 1.
DR Pfam; PF17998; AgI_II_C2; 2.
DR Pfam; PF16364; Antigen_C; 2.
DR Pfam; PF08363; GbpC; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF19258; KxYKxGKxW_sig; 1.
DR SUPFAM; SSF74914; SSF74914; 1.
DR TIGRFAMs; TIGR04228; isopep_sspB_C2; 3.
DR TIGRFAMs; TIGR03715; KxYKxGKxW; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Cell wall; Direct protein sequencing; Peptidoglycan-anchor; Plasmid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..43
FT /evidence="ECO:0000269|PubMed:2120541"
FT CHAIN 44..1264
FT /note="Aggregation substance"
FT /id="PRO_0000005593"
FT PROPEP 1265..1296
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000005594"
FT REGION 48..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1261..1265
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 48..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1264
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1296 AA; 142285 MW; 52123A133AD23E5B CRC64;
MKQQTEVKKR FKMYKAKKHW VVAPILFIGV LGVVGLATDD VQAAELDTQP GTTTVQPDNP
DPQVGSTTPK TAVTEEATVQ KDTTSQPTKV EEVASEKNGA EQSSATPNDT TNAQQPTVGA
EKSAQEQPVV SPETTNEPLG QPTEVAPAEN EANKSTSIPK EFETPDVDKA VDEAKKDPNI
TVVEKPAEDL GNVSSKDLAA KEKEVDQLQK EQAKKIAQQA AELKAKNEKI AKENAEIAAK
NKAEKERYEK EVAEYNKHKN ENGYVAKPVN KTLIFDREAT KNSKVVSVKA AEYIDAKKLT
DKHKDKKLLI SMLSVDSSGL TTKDSKKAHF YYNNGAGGTL VVLHKNQPVT ITYGNLNASY
LGKKIASAEF QYTVKATPDS KGRLNAFLHD DPVATIVYGI NIDPRTKKAG AEIEMLVRFF
GEDGKEILPT KENPFVFSGA SLNSRGENIT YEFVKVGNTD TVHEINGSKV ARHGNKVYSK
TDIDVGTNGI SISDWEAVQG KEYIGATVIS TPNRIKFTFG NEIVNNPGYD GNSMWFAFNT
DLKAKSITPY QEKGRPKQPE KATIEFNRYK ANVVPVLVPN KEVTDGQKNI NDLNVKRGDS
LQYIVTGDTT ELAKVDPKTV TKQGIRDTFD AEKVTIDLSK VKVYQADASL NEKDLKAVAA
AINSGKAKDV TASYDLHLDQ NTVTAMMKTN ADDSVVLAMG YKYLLVLPFV VKNVEGDFEN
TAVQLTNDGE TVTNTVINHV PGSNPSKDVK ADKNGTVGSV SLHDKDIPLQ TKIYYEVKSS
ERPANYGGIT EEWGMNDVLD TTHDRFTGKW HAITNYDLKV GDKTLKAGTD ISAYILLENK
DNKDLTFTMN QALLAALNEG SNKVGKQAWS VYLEVERIKT GDVENTQTEN YNKELVRSNT
VVTHTPDDPK PTKAVHNKKG EDINHGKVAR GDVLSYEMTW DLKGYDKDFA FDTVDLATGV
SFFDDYDETK VTPIKDLLRV KDSKGEDITN QFTISWDDAK GTVTISAKDP QAFILAHGGQ
ELRVTLPTKV KANVSGDVYN LAEQNTFGQR IKTNTVVNHI PKVNPKKDVV IKVGDKQSQN
GATIKLGEKF FYEFTSSDIP AEYAGIVEEW SISDKLDVKH DKFSGQWSVF ANSTFVLADG
TKVNKGDDIS KLFTMTFEQG VVKITASQAF LDAMNLKENK NVAHSWKAFI GVERIAAGDV
YNTIEESFNN EKIKTNTVVT HTPEKPQTPP EKTVIVPPTP KTPQAPVEPL VVEKASVVPE
LPQTGEKQNV LLTVAGSLAA MLGLAGLGFK RRKETK
