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
//