ID A0A0K1XBH8_9GAMM Unreviewed; 1635 AA.
AC A0A0K1XBH8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=AKN88_01460 {ECO:0000313|EMBL:AKX58740.1};
OS Thiopseudomonas alkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Thiopseudomonas.
OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX58740.1, ECO:0000313|Proteomes:UP000063953};
RN [1] {ECO:0000313|EMBL:AKX58740.1, ECO:0000313|Proteomes:UP000063953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E5571 {ECO:0000313|EMBL:AKX58740.1,
RC ECO:0000313|Proteomes:UP000063953};
RX PubMed=26679585;
RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA Juieng P., Loparev V., McQuiston J.R.;
RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT a Novel Bacterium of the Pseudomonadaceae Family.";
RL Genome Announc. 3:e01474-15(2015).
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; CP012365; AKX58740.1; -; Genomic_DNA.
DR RefSeq; WP_053099649.1; NZ_CP012365.1.
DR STRING; 1697053.AKN87_03560; -.
DR PATRIC; fig|1698449.3.peg.290; -.
DR Proteomes; UP000063953; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; IPR011626; Alpha-macroglobulin_TED.
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 Pfam; PF07678; TED_complement; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000063953}.
FT DOMAIN 732..880
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 944..1032
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1635 AA; 179732 MW; 46497A22FE35D9E7 CRC64;
MKYLAILTFI ASLLVLQGCD SEQATPPATT KSNDLLEPRQ PLTAEARAHL IAEYQQQPLT
VQNVEETQFQ GSNALQVSFS APLADTVDLA QYLVLADSEQ GRLESSWVLA ESLTEAYFLD
LPPATKLQLQ IKAGLPGLAG QILNKEYQQQ LTSNDLQAVV GFASKGSLLP EAMAEGLPII
SLNVDQVEVD FFRVKADKLL PFISQWSDNN RLELWQAESL LKMAELVYSG RFALETTTNT
REQSLLPLAG IKPLSEAGLY FAVLRPAGDY SYSLPATVFS ISNIGLSVHQ SAQYLDIFSQ
NLTQGAGMSK VEVRVLDQAG KTLEQGLTDS QGILRLNAAP KAAAVIATYQ QQTSIVRLDR
AALDLSAFDL SGAEAGAMQL YLFAARDLYR PGEQVTVNLL LRDSDGQLLG EQPIKLRVKR
PDGLVTADKT YIVSKGFLQE TIALSQGAPV GRWALEAELG NGQVSHYEFS VEDFLPERMA
LDLTPDRPVL TGETDLVITV KGRYLYGAPA DGNSVEAQAR VVPLRQPFAE LKGFEFGLVD
AKPSDNFTLN SVRLDAQGQG QLSLNVQWQN LDSPAQLQTQ VSLLESSGRA LTRTLQQPIF
PTEQLIGIHS LQGNELEENT EAEFELLLTD RDGQALNSGE LTVKLYQERR DYYWSYSESQ
GWSSKYHAQD ILQERQQIKL TDAQSVGIKL PVKWGSYRLE VALEGSSVSS SQRFWAGYRW
QGDSQGLKPD QVALSLDQPA YQVGDVAKIS VQSPHAGQGY LLLESQQGVL WQQPISLTTE
TRVIELPIAE QWKQHDLYIS ALVVRPGAKK ADATPKRAIG LIHLPLARAD RQLQVQLAHA
EQVRPLQNLT TKVQVLQADG QPARQAKVLL SAVDSGVLSI TDFNTPDPFA GFYGRKKYAI
DQYDVYHQLI DASQGKLAKL KFGGDAEEDQ AGAMRALAKP VIVSLQNEVV QLDEQGQATI
TLAMPDFNGE LRLMAQAWQE DQFGATDSLT KVVAPVVAEL AMPRFIGSGD QVQAMLELTN
LSAETQQVQL QLSATGLLQL TAVEVQQLTL KPQQRQVIPV ALTGHYGFGE GAVNLILSGI
ELADEDYSQL TKHWPITVRP NSKEQKRIYG QLLQPDETWT LAENAHQGLL LQGATLGLSA
ALEPPLQINQ QIKQLAEYPY DCAEQTVSRA LPLLYLSRAD LEQALTVTQA DAYQAQLQYG
VERLLSLQDY NGGFSMWSRS GAEQPWLTVY ATEFLQLAQN KGALVPSAAL TKAEQRLARY
IQESYLIDSE ATENLSHYRF AVQAYAGYVL AQQGKVNLGQ LRELFERRTE AVAPVPLLQL
SRALSLMGDQ DRALEALSLG LQLQRPARQW LGDYGTELSD LATMLPLLVE AKASSAAIGQ
RLQQLSAQLM RQSWLSTQER AAIIKAAASL NLLPSARDQA AGFELSVTQA GQSHSLPAQR
SLEQVFAYTE GFSVTNRSEQ AVYLQLALSG YPKSVEQAVQ SQSLSIERQY FDQAGQPLDL
TQVESGQLLV VHLAVRSSQS IPDLLVEDLL PAGLEIENQN LDRVSASLDS VTGELKTWLN
AMESSYLEYQ AALDDRYVAS FNLSADSTQH LLYLARAVSP GAYRLAAPRA ESMYRPELQA
QGATPKWLTI VPRRS
//
