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FM1_ACTVI
ID   FM1_ACTVI               Reviewed;         533 AA.
AC   P18477;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Fimbrial subunit type 1;
DE   Flags: Precursor;
OS   Actinomyces viscosus.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae; Actinomyces.
OX   NCBI_TaxID=1656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-56.
RC   STRAIN=T14V;
RX   PubMed=1970561; DOI=10.1128/jb.172.5.2462-2468.1990;
RA   Yeung M.K., Cisar J.O.;
RT   "Sequence homology between the subunits of two immunologically and
RT   functionally distinct types of fimbriae of Actinomyces spp.";
RL   J. Bacteriol. 172:2462-2468(1990).
CC   -!- FUNCTION: Major fimbrial subunit of A.viscosus.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}. Fimbrium.
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DR   EMBL; M32067; AAA62572.1; -; Genomic_DNA.
DR   PIR; A35259; A35259.
DR   PDB; 3UXF; X-ray; 1.60 A; A=31-491.
DR   PDBsum; 3UXF; -.
DR   AlphaFoldDB; P18477; -.
DR   SMR; P18477; -.
DR   PRIDE; P18477; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR026466; Fim_isopep_form_D2_dom.
DR   InterPro; IPR032364; GramPos_pilinD1_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF16555; GramPos_pilinD1; 1.
DR   TIGRFAMs; TIGR04226; RrgB_K2N_iso_D2; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Direct protein sequencing; Fimbrium;
KW   Peptidoglycan-anchor; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:1970561"
FT   CHAIN           31..499
FT                   /note="Fimbrial subunit type 1"
FT                   /id="PRO_0000005601"
FT   PROPEP          500..533
FT                   /note="Removed by sortase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT                   /id="PRO_0000005602"
FT   MOTIF           496..500
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   MOD_RES         499
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          81..88
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   HELIX           94..102
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          114..122
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          138..147
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          158..165
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          173..179
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          188..193
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          204..211
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   TURN            217..220
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          227..232
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          244..251
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   TURN            258..260
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          261..267
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          269..278
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   HELIX           280..291
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          298..305
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          314..324
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          346..348
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          352..365
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   HELIX           372..375
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          379..388
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          391..394
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   TURN            419..421
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          422..429
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          446..454
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          466..468
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   HELIX           472..475
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   TURN            476..478
FT                   /evidence="ECO:0007829|PDB:3UXF"
FT   STRAND          481..487
FT                   /evidence="ECO:0007829|PDB:3UXF"
SQ   SEQUENCE   533 AA;  56900 MW;  F00299559C702FC4 CRC64;
     MHSLNTRRGL GLAAAMTLAA GALVAPTGAA APADPNGSTI DPDAATTLTV HKCEQTDTNG
     VKEGTGNEDP QAECKPVSDV EFTITKLNVD LTTYDGWKTL ADLKGDVVKA GALKSTTVQK
     ITTGANGLAS FTDAQTEVGA YLVSETRTPD KVIPAEDFVV TLPMTNPQDT AKWNYNVHVY
     PKNTLSGVDK QVTDKPAPGS GRDITYTITT SIPKVDYPGG ARIKRYEVVD RLDKRIKKEA
     LTPVVKIVGQ NEVTLAETTD YTLITAEGKD HNWATIQLTE EGRRKASEAR YNGNGETKLQ
     VTLNAKFDAA VNLEGDLSNT AGLIPNDSPN FTWDPNNPGT TTDIPGIPTT PVLSKYGKVV
     LTKTGTDDLA DKTKYNGAQF QVYECTKTAS GATLRDSDPS TQTVDPLTIG GEKTFTTAGQ
     GTVEINYLRA NDYVNGAKKD QLTDEDYYCL VETKAPEGYN LQADPLPFRV LAEKAEKKAA
     TEVTVTDIPK NAGFRLPLTG ANGVIFLTIA GALLVAGGAV VAYANKRRHV AKH
 
 
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