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Database: UniProt
Entry: A0A089ZQX0_9PSED
LinkDB: A0A089ZQX0_9PSED
Original site: A0A089ZQX0_9PSED 
ID   A0A089ZQX0_9PSED        Unreviewed;      1634 AA.
AC   A0A089ZQX0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN   ORFNames=LT40_13655 {ECO:0000313|EMBL:AIS18366.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS18366.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS18366.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS18366.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT   a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL   J. Biotechnol. 193:137-138(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; CP009533; AIS18366.1; -; Genomic_DNA.
DR   RefSeq; WP_043190968.1; NZ_CP009533.1.
DR   STRING; 216142.LT40_13655; -.
DR   KEGG; prh:LT40_13655; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_000965_1_0_6; -.
DR   Proteomes; UP000029499; 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:UP000029499};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1634
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001852589"
FT   DOMAIN          736..884
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          947..1036
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1634 AA;  178356 MW;  ED3DF57D0E85B7B6 CRC64;
     MNKGLFLACA LALLGGCDSS TAEKPVEPSP PVAATATANP GAVVDLPALA KRYEGRELTV
     ADASEIQLDG ASTLSLTFSA PLDPQQNFAD KVHLVDSTRG KLDGAWELSD NFMELRFRHL
     EPKRKLVLTV DAGLLSVNRT TLATSYTSRL ETQDLQPTVG FASRGSLLPT RLAEGLPVIA
     LNVDKVDVEF FRIRPEQLPA FLSRWGRNSS LQSYESRELL PMAELVYGGR FDLDPARNTR
     ETLLLPIAGI EPLQQPGVYL AVMRASGTYD YAQPATLFTL SDIGLSVHRY ADRMDVFTQA
     LEGGKALADV SLQLLDGKGR VIGEGKTDAA GHAELPSPVK AEVLLAHLGE QTSLLRLNTA
     ALDLAEFDIA GPKAHPLQFF VFGPRDLYRP GETVLLNALL RDNDGHPVKP QPVNVEVRRP
     DDQLSRKFVW QPDESGLYRY QLPLAGEAPT GRWQLLLDLG DGKPQVYEFQ VEDFLPERMA
     LELKGQDMPI APADALNVDV TGRYLYGAPA SGNRLSGQVY VRPLREAVPA LPGFQFGSLT
     EGELSQDLEL DEATLDAQGK TNLAIDSRWS EARSPLQVVL QASLQESGGR PITRRLVQPV
     WPADRLPGVR GMFDGENVDG DGPAEFEVLV ADAQGHKLAA DALKVRLVRE RRDYYWNYSE
     SDGWSYNYNE KYLNLSEETL SVAEGTTAKV SFPVEWGPYR VEVEDPQTGL VSSLRFWAGY
     SWQDNTEGGA VRPDQVKLAL DKPHYGDGDT ARVTVTPPAA GNGYLLVESA EGPLWWQEID
     VPAEGKTFDI KVDPKWARHD LYISALVIRP GERKANVTPK RAVGLLHLPL DRAARKLALT
     LDAPATMRPQ QPLTVKVQAR NSDGSIPRQA HVLLAAVDVG ILNITQYATP DPFAALFGRK
     GYGADQLDIY GQLIEAGQGR LASLAFGGDA ADLAKGGKRP PTSVNIVALQ STPVTLDERG
     EGQLTVDIPD FNGELRLMAQ AWTEDRFGMA EAKTVVAAPL VAELSAPRFL AGGDQARIAL
     DVTNLTERAQ TLTVQLNTEG PLTLVDAPRK QLQLAKGERQ TLYVQVQASG GLGQGHIKVL
     IDGIDLPGET LPPIARNWTL GVRPPYPALV SHLRSVLKDQ QPWTLPAGAL SPFEPAGREA
     LLTLSSRPPL NIGEQIKALR AYPYGCLEQT VSGLYPSLYS DAASLEKLGV GGDTDAERKR
     KMEVGIERLL GMQRYNGSFG LWSAEGEEEY WLTAYVTDFL LRARDQGYAV PPEPLKKAGE
     RLLRYLQERD LIEADYSDNL EHTRFAVQAY AGLVLARSQQ APLGALRSLF ERRTDARSGL
     PLVQLAIALQ KMGDQPRADQ ALQAGLAAGR SDNEWLGDYG SPLRDQALVL ALLQENELSK
     PTLEQRLFTL SDLLASSSWL STQERNAVYL AGRNALAKPQ QPWTAQLQSA GASHQLSDTQ
     PALKLAGSAL SESLTVSSEA QQPLYQQLTL SGYPVRPPAL HADTLSIRRQ YLGLDGEPLK
     LDTLKSGDLV LVHLAVSAKQ RVPDALVVDL LPAGLEIENQ NLAQSAASLD SAGSNVRQWR
     ESMQNASLQH QEFRDDRYVA ALKLEGYGST HLLYLARAVT PGTYKVPPPQ VESMYRPNWQ
     AVGATPSDLT VRPR
//
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