ID B8L9N3_9GAMM Unreviewed; 1635 AA.
AC B8L9N3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=SSKA14_1834 {ECO:0000313|EMBL:EED38820.1};
OS Stenotrophomonas sp. SKA14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=391601 {ECO:0000313|EMBL:EED38820.1};
RN [1] {ECO:0000313|EMBL:EED38820.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA14 {ECO:0000313|EMBL:EED38820.1};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protects the bacterial cell from host peptidases.
CC {ECO:0000256|PIRNR:PIRNR038980}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000256|ARBA:ARBA00010556}.
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DR EMBL; DS999412; EED38820.1; -; Genomic_DNA.
DR RefSeq; WP_008266186.1; NZ_DS999412.1.
DR HOGENOM; CLU_000965_1_0_6; -.
DR Proteomes; UP000003991; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR CDD; cd02891; A2M_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR InterPro; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR040639; A2MG_MG1.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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 PANTHER; PTHR40094; ALPHA-2-MACROGLOBULIN HOMOLOG; 1.
DR PANTHER; PTHR40094:SF1; UBIQUITIN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF21142; A2M_bMG2; 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 SMART; SM01419; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Protease inhibitor {ECO:0000256|PIRNR:PIRNR038980}.
FT DOMAIN 741..884
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 948..1037
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1635 AA; 178172 MW; 0C5D4DAE565956A1 CRC64;
MSGPARRKRW GWAAAVLAGG LLLGLAGCRN DSGQLPKASG EAITTKAEQV KEFTLLRAYP
DQKNDGLSLA LEFSRPLVGT QDFDKLVRFE EKVGTDDSSW TLSDDGLTLR YPFVEAGKEF
SLVVSADLLA ADGSRLGKEL KQKVFSGELK PVVGFASQGS VLPAKDSRGL PVVSVNVPEV
DVEFLRVREK DLPTFFSQYQ RGGRRGSWEL SSDYERSPIN KLAEPVYVNR FILGGKQNER
VLTYLPTQDI KELQEPGLYF ALLKRTGDYE GEFDTAFFSV SDIGLHTRAY KDKLFVHTAG
LKDGAPLKGI DLRVLDAKGE VVLKGSTDGN GNALLNYTLD ATHVLVASSG KDTSFLPFNQ
PALDLSEFAV AGRDNAWFDV YAWSGRDLYR PGETVRLSAL LRDNDGKPVK AQPVFLRLKQ
PDGKTFRETR LQPGDQGYIN FEQAIPAEAP TGRWQVEFRT DPASKEAIQG MTLRIEEFLP
ERMKLDLDSA QKTLKPGEEL RLQANGAYLY GAPADGNRFT ARMAVAAEQK PVDGLPGYFF
GDPTLQLPRE AKDVIDTTMP ANGQLREDVA LPEEAAKAKA PIAVVLSGSL YETGGRTVTR
TLKRVMWPAN ALVGVRPLFN PDDGADSNGN ARFELMRVDA AGNPQPAKGL KITLVRELRD
YHWTFNDNRW DYDFTRRFEN KETRTVDAGS SAVAFDFPVE WGEYRVDVFD PSTGLTSRYP
FRAGWSWGDD NRGLDARPDK VKLGLDKTGY KAGDTLEVTV TPPHAGKGIL MVETDRMLYV
QDIEAKPGST FKIPVTADWE RHDVYITALV FRGGSAPSKI TPARAVGVVH VPMDRKGRTV
AVGLVAPKQM RPEQDLPVTV SAPQLAGKTA HVTVSAVDVG ILNITRFPVP DAGAHFFAQR
RLGIDAYDIY SRVIESFDGG AGKLKFGGDM ALQALPQAKR PTARVQTVDL FSGPVQLDAK
GIARIRLKVP DFNGTLRVSA LVYSDDQYGK RDVETVVRAP ILAEASMPRV LAPGDRSTVT
LDVQNFTGKP GQFNVKVESE GPLNLGEGSR SVQLNADAKT TLSFPLSARE GHSVAKVRVR
VDGNGFKADR RYDLPVRAAW PQVLRSQVRT LDPLAAVSLD NSLTDGLMSE SVNARLLVSP
LPPIPFASAL QGALNYPYGC AEQTTSKGYA ALILDQATSS MLGADGLDAK TRRERMEGAF
GRLASMQVAN GNFSMWGDDG YVNPWLTPYI TEFLLDAKDA GFAVPDNVLQ KALNRLSEDL
LSGGNQFYGQ DDREKLKFAN QAYSGYVLAR VNRAPLGTLR TLYDNERSKA VGGLSLVHLG
VALSLQGDAK RGQAALAAAF AKSSSERPSY FGDYGSAIRD DALMIALTHE NKLAKPAWDA
RAVDLGRGLD ARRNAGWMWL STQEQVAIAR LGKALAANQK ALVAGELVIG GTTEAISERK
LFGRNFSASE LASGVRFTPQ GQPPMFASID VAGIPRSAPA PDNSVLGIER SYYGTDGKPW
SPRPLKEGEA LIVRVTVTAD TTMPDALLTD LLPAGLEIEN FNLGDAKQWA DVVVDGITIS
DRGEAADTKH EEFRDDRYVA ALKLSRGSKA SVFYLVRAVT PGTYSVPPPL VEDMYRPQLR
GVGRSNPTTI TVVQP
//
