ID   A0A1I3LHI5_9PSED        Unreviewed;      1640 AA.
AC   A0A1I3LHI5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN   ORFNames=SAMN05216206_2958 {ECO:0000313|EMBL:SFI84212.1};
OS   Pseudomonas guineae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=425504 {ECO:0000313|EMBL:SFI84212.1, ECO:0000313|Proteomes:UP000243606};
RN   [1] {ECO:0000313|Proteomes:UP000243606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24016 {ECO:0000313|Proteomes:UP000243606};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FOQL01000004; SFI84212.1; -; Genomic_DNA.
DR   STRING; 425504.SAMN05216206_2958; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000243606; Unassembled WGS sequence.
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:UP000243606};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1640
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017208165"
FT   DOMAIN          737..885
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   1640 AA;  179464 MW;  DAF09DED04A1C699 CRC64;
     MPKNGLLLAL VLSLLSACDS SAPEPAEVTA TQATPVSDET AKPALDLKAL AERYAGRELS
     VVDVSEVQLE GASTLSISFS VPLDPEQKLA ERLHLVDSKS GKVDGAWELA DNLMEVRLRH
     LEPQRKLVLT VDAGLLALNG ERLADEQVSR LETRDLQASV GFASRGSLLP TRLAEGLPVI
     ALNVDKVNVE FFRIKPESLP AFLNRWGRSS NMDNWESRSL LPMADLVYGG RFDLNPARNT
     RETLLLPIAG LEPFKQPGVY LAVMREAGSY NYSQPATLFT LSDIGLSARR YQNRLDVFTQ
     ALAGGDALGD VRLEILNGEG QVLAEGETDS AGHAELPLPA KAEVLLAHQG EQTSLLRLNS
     SALDLAEFDI AGPVAHPLQF FVFGPRDLYR PGETVLLNGL LRDADGRALK AQPVNVEVRR
     PDEQVSRKFV WQADDAGLYQ YQLQLADEAP TGRWQLLFEL GDGKPQLYEF SVEDFLPERM
     ALEIKGSEEP YTPAENAQFE VTGRYLYGAP AAGNRLSGQL YVRPLREAVA SLPGYQFGSV
     TEEELSEDIE LDETSLDEQG NASLDIESRW ADAKSPLRLI LQASLQESGG RAITRRLIQP
     VWPAERLPGV RGLFDGEEVD ADSLAEFEVL VADAAGNKLA AEQLSVRLIR ERRDYFWNFS
     ESDGWSHNYN EKFLTLNEET LEVAAGGTAK ISFPVEWGPY RVEVVDAQTG LLSSLRFWAG
     YRWQDNADGG AVRPDQVKLA LDKPAYVDGE TAQVTVTPPT AGKGYLMVES SDGPLWWQEV
     DVPAEGKTFA IPIAKDWARH DLYVSALVIR PGERKSNATP KRAVGLLHLP LERAPRKLAL
     TLTAAEKIRP NQPLTVKVRV RNADGSMPKH AQVLVAAVDV GILNITEYAT PDPFANFFGR
     KAYGADQLDI YGQLIEAGQG RVAKLAFGGD AALAAGGKRP DTSVLIVALQ SQPLALNEQG
     EGEVSLAIPD FNGELRLMAQ AWTDEHYGMG EGKTVVAAPL IAELSAPRFL AGGDETTLAL
     DLNNLSGREQ TLDVQLSAEG QLRLAQSPGV AVAPITLADG QRTILRIPVV ALGGYGKGQI
     KVSVNGLELP GETLPPFSRE WQLGIRPAYP AQLQHFRAVL KDEPWLLPAD ALSAFESAGL
     EARLAISSRP PLNLGEQIRA LKAYPYGCLE QTTSGLYPSL YADAATLKRL GVEAEPDEQR
     KRAIELGIER LLSMQRYNGS FGLWGADGDE EYWLTAYVSD FLLRAREQGF GVPEEALKKA
     NERLLRYLQE RQLIEVNYSD NANHSRFAVQ AYAAYVLARS QQAPLGALRS LYERRSDALS
     GLPLVHLAVA LQKMGDQPRA DELLTAGLAR GRESNTWLAD YGSPLRDQAL ILALLEEHDL
     ASDRREQRLF NLADEVAGQQ WLSTQERNSL YLAGRNLLST PEPSWSAQLQ SASLAFELSK
     AQSGLKLEGR DLAAPLSISN STSKPGDTPL YQQLTLSGYP SQAPTAGGEN LSIYREYLGM
     DGRKLDLSNM RSGELVLVHL AVSAKQRVPD ALVVDLLPAG LELENQNLAQ SAASLDDASS
     AVKEWRESMQ NAAIKHQEFR GDRYVAAVDI NGYDTTHLLY LARAVTPGSY RVPPPQVESM
     YRPNWQALGE TPGRLIVKER
//