ID A0A077LDA2_9PSED Unreviewed; 1653 AA.
AC A0A077LDA2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=PSCI_1124 {ECO:0000313|EMBL:BAP41826.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP41826.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP41826.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP41826.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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; AP014637; BAP41826.1; -; Genomic_DNA.
DR RefSeq; WP_045483944.1; NZ_AP014637.1.
DR STRING; 1028989.PSCI_1124; -.
DR KEGG; pses:PSCI_1124; -.
DR HOGENOM; CLU_000965_1_0_6; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000031652; 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 Lipoprotein {ECO:0000313|EMBL:BAP41826.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Protease inhibitor {ECO:0000256|PIRNR:PIRNR038980};
KW Reference proteome {ECO:0000313|Proteomes:UP000031652}.
FT DOMAIN 755..903
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 964..1053
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1653 AA; 180353 MW; 1F3856F556067DE1 CRC64;
MLNKGLFLAC ALALLSACDS SSPDKPAAPP AQTSTPAAAA TTKPKPAVDL PALAKRYTGR
EVSVVDVSEI QVEGASTLSV SFSVPLDPEQ KFAEKLHLVD SKTGKVDGAW ELSDNLMELR
LRHLEPQRKL VLTVDAGVRG VNNNTLASEF SARLETRDLQ ATVGFASRGS LLPTRLAEGL
PVIALNVDKV DVEFFRVKPD QLPNFLTEWE GSSSMSAYRS EQLLPMADLV YGGRFDLKPA
RNTRETLLLP IGGIKPLQEP GVYLAVMRAS GSYNYTLPAT LFTLSDIGLS VHRYSQRLDV
FTQALEGGKA QSDVNVDVYD NDGKVVAQGK TDGKGHAQLP LPNKAALILA HKGEQTSLLR
LNSPALDLAE FDISGPQAHP LQFFVFGPRD LYRPGETVLL NGLLRDQDGK SVKTQPINVE
VRRPDEQVSR KFVWEPDASG LYQYQLQLAD EAPTGRWQLV YDLGDGKPQL YEFNVEDFLP
ERLALDLKGS ETPISPEQNP QFEITGRYLY GAPASGNSLT GQLYVRPLRE AVEKLPGYQF
GSITEEDLKF DRELDATTLD ANGEAVLDVQ TEWAKARSPL NVILQASLQE SGGRPITRRV
VQPVWPAERL PGLRALFGSS TGEDDYGYGA ARGEAQTDGD GPAEFEILVA DAAGNKLAAN
DVKVRLVRER RDYYWTYSDS DGWSYNYNEK FLNLSEETLT INKDATAKVT FPVEWGPYRV
EVEDPATGLV SSLRFWAGYR WQDNAEGGAV RPDQVKLALD KPAYADDATA RVTVTPPAAG
KGYLLVESSE GPLWWQEIDV PAEGKTFDIQ LDKKWARHDL YVSALVIRPG ERKANVTPKR
AVGVLHLPLD RSQRKLGLTV TAPEKMRPKQ PLKLKVAAKN ADGSVPKQVQ VLVSAVDVGI
LNITRYATPD PFASLFGRKE YGADQLDVYG QLIEAGQGRL ASLAFGGDAL AKGGKRPDTS
VTIVALQSAP VVLNEQGEGE VSVDIPDFNG ELRIMAQAWT DERYGMAEAK TVVAAPLIAE
LSTPRFLAGG DQTSVALDLA NLSGKAQKLD VQLFAEGQLS IPGGDQSKTV QLQQGQRTTL
KFPVQAQGGL GQGKLRVKVD GLVIPGEDLP PLSREWTVGV RPAYPAMLRH FRAVLEPGQE
WSLPEGALQA FEPAGREALM SLSSRPPLNL GEQIRALKAY PYGCAEQTAS GLYPSLYADA
ATLKRLGLAG EPDAERKRKV EIGIERLLGM QRYNGSFGLW GADGEEEYWL TAYVTDFLLR
ARDQGFAVPA EALKKANERL MRYLQDRGQV QVNYSQNAEH TRFAVQAYAG LVLARSQQAP
LGALRTLFER RSDARSGLPL VQLAVALEKM GDKPRAEQAL RAGLAAGRKP NEWLADYGSP
LRDQALILAL LEENNLGGEA RNQRLFDLAD QLAASRYLST QESNSLFLAG RNLLGKPEKD
WTALLSSAGQ NLDLSNRQPG QKLAGAVLAA PLALHNQSGE TLYQQLTLSG YPTQAPLAGG
ENLTISREYL SLSGQPLNVE ALKTGQLVLV HLQVSARQRV PDALIVDLLP AGLELENQNL
AQSAASLEDA SESIKGFRES MENASLKHQE YRGDRYVAAL DIEGSTRPVH LLYLARAVTP
GIYKVPPPQV ESMYRPNWQA LGEAPAQMVV RAK
//
