A2MG_XYLFT
ID A2MG_XYLFT Reviewed; 1641 AA.
AC Q87E11;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000250|UniProtKB:P76578};
DE Flags: Precursor;
GN OrderedLocusNames=PD_0518;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
CC -!- FUNCTION: Protects the bacterial cell from host peptidases.
CC {ECO:0000250|UniProtKB:P76578}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000305}.
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DR EMBL; AE009442; AAO28391.1; -; Genomic_DNA.
DR RefSeq; WP_011097675.1; NC_004556.1.
DR AlphaFoldDB; Q87E11; -.
DR SMR; Q87E11; -.
DR MEROPS; I39.008; -.
DR DNASU; 1144721; -.
DR EnsemblBacteria; AAO28391; AAO28391; PD_0518.
DR GeneID; 58016065; -.
DR KEGG; xft:PD_0518; -.
DR HOGENOM; CLU_000965_1_0_6; -.
DR OMA; LDRYPYG; -.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR040639; A2MG_MG1.
DR InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR InterPro; IPR041203; Bact_A2M_MG5.
DR InterPro; IPR041462; Bact_A2M_MG6.
DR InterPro; IPR041246; Bact_MG10.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF17970; bMG1; 1.
DR Pfam; PF17973; bMG10; 1.
DR Pfam; PF11974; bMG3; 1.
DR Pfam; PF17972; bMG5; 1.
DR Pfam; PF17962; bMG6; 1.
DR Pfam; PF01835; MG2; 1.
DR PIRSF; PIRSF038980; A2M_bac; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Protease inhibitor;
KW Signal; Thioester bond.
FT SIGNAL 1..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 32..1641
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000036247"
FT LIPID 32
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 32
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CROSSLNK 1166..1169
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250|UniProtKB:P76578"
SQ SEQUENCE 1641 AA; 179071 MW; 26DB567618C9A03A CRC64;
MRDRVAMMLR PLVRGWIPRA VLLLTVAFSF GCNRNHNGQL PQSSGEPVAV AKEPVKGFVL
VRAYPDQHDG ELALALEFSQ PLAATQEFDT LVRLEQGSGN HDGGWSLSDD AKTLRYPYVE
ADKHYTVLIS GDLLAATGSR LGKSRKEPVY TGELDPVVGF ASRGSILPAR GSRGVPVVSV
NVPEVDVEFM RVREKALPAF LARYHKAGQR SSWELSNQGN SRKRLSELAD PVYVTRFVLD
GKKNERALTY LPIQNIRELR EPGLYFAVMK PTGSFSDAFE TAFFSVSNIG LHARAYKDKL
FVHTASLRSG NPYKQVDLLV LDAKGETVLQ GATDDNGNAL LNYTLNAGHV LVSRNGRDIS
ILPFNQPALD LSEFAVAGRE NPWFDVFAWS GRDLYRPGEM LRISALLRDR DGKPVKPQPV
FLRLKQPDGK TFRETRLQPA EQGYLEFTQK IPSDAPTGRW RVEFRTDPAS KEAVQGLAVR
VEEFLPERMK LELSSAQPVL RAKAPFTLTA DAAYLYGAPA AGNRFTANLA VAVEQHPLDN
MPGWFFGDAT LQLPRGAKET IDITLGADGH LVHDIVLPEE AKPVSPMAVV VSGSVYESGG
RPVTRSLKRV LWPADALVGV RPLFDVASGA DANGMARFEL TRVGVDGKPQ SAKGLKATLV
RELRDYHWRY SDGRWDYDFT RRFENKETRT VDISSSHTTT LSLPVEWGDY WLEVFDPVTG
LTMRYPFRAG WSWGDDNRGL DARPDKVKLA LDKTSYRAGD TLKVTITPPH PGKGLLLVES
DKPLYVQAID ANPSTTLEIP VTADWERHDV YVTALVFRGG SASNNTTPAR AVGEAYVPMQ
RKERRVAVGL VVPKQVRPAQ SLPVTVSVPE LAGKQAHVTI SAVDAGILNI TGFPVPDAAA
HFFAQRRLSV DAYDIYGRVI ESFEGGTGRL KFGGDMALPP LPQAKRPTAR SQTVDLFSGA
VKLDAKGNAH IQLPVPDFNG ALRVSALVYS DTRYGQRDAE TVVRAPILAE ASMPRVMAPG
DRSTVTVDVQ NFTGKQGKFA VKVEGVGPLV VAEAGRSVTL GIDGKTTLNF PLRALEGNSV
AQVRVRVEGN GSKAERHYDL PVRAVWPQGL RTQAHVLNVL APIAFDPALA KGLMPDSVNA
RLSVSTLAPI PFASVLQGVF EYPYGCAEQT ASKGYAALWL DDATIRSLGI QGVTPAQRLE
RLEGALGRLA SLQTTNGHFS MWGGNSDVNP VLTPYIAGFL LDAKDAGFAV SDAVLQKALN
RLSEDLLSGA HLFYGNDQSE ALMFAHQAWS GYVLARVNRA PLGTLRTLYD NERGKAVSGL
SLVHLGVALS LQGDRKRGEA AIEAGFAKSE GGRPEVFGDY GSVIRDNALM IALVRAHGLA
KPAYEARVMA LGRDLQARRR SGWLWLSTQE QVALAQLGRA LLVDQKKQVS GTLYVGKQRE
DIAASRLIGR SFDAAALARG VRFVPQGDVP LYASFEVAGI PRQAPVSDDS QLLVVRRWYT
VDGKPWTPGP LKEGQALIVR VSVTSKQNMP DALLTDLLPA GLEIENFNLG ETRQWADVTV
DGIALSERAD AADIKHEEFR DDRYVAMLQL TGGRTANLFY LVRAVTPGSY NVPPSLVEDM
YRPALRGTGR VAPAMVTVVQ P
