ID A0A089WL56_9PSED Unreviewed; 1633 AA.
AC A0A089WL56;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=LK03_08610 {ECO:0000313|EMBL:AIR89336.1};
OS Pseudomonas cremoricolorata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR89336.1, ECO:0000313|Proteomes:UP000029493};
RN [1] {ECO:0000313|EMBL:AIR89336.1, ECO:0000313|Proteomes:UP000029493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND07 {ECO:0000313|EMBL:AIR89336.1,
RC ECO:0000313|Proteomes:UP000029493};
RA Chan K.-G.;
RL Submitted (SEP-2014) 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; CP009455; AIR89336.1; -; Genomic_DNA.
DR RefSeq; WP_038411924.1; NZ_CP009455.1.
DR STRING; 157783.LK03_08610; -.
DR KEGG; psw:LK03_08610; -.
DR eggNOG; COG2373; Bacteria.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000029493; 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; IPR049122; A2MG_CUB.
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; PF21765; A2MG_CUB; 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:UP000029493};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1633
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001850997"
FT DOMAIN 738..886
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 948..1037
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1633 AA; 178202 MW; 7C58B4E001A502B6 CRC64;
MFNKGLLLAC ALALLSACDS STSEQPAPAA KPAAASPAAA PAAKREDPAV LAKRYAGREL
NVLDVSEVQI DGASALSVSF SAPLDAEQDF AAKLHLVDTV KGKVDGAWEL SDNQMELRLR
HLEPQRKLVL TVDKGLLGVN GKTLADELVS RLETRDMQAT VGFASRGSLL PTRLAEGLPV
IALNVDKVDV EFFRVKPEML SSFLAGWGRN SSLYYYQSKE TLAQADLVYS GRFDLNPARN
TRETVLLPIA GIKPLQEPGV YLAVMRASGT YDYSQPATLF TLSDIGVSAH RYRDRIDVFT
QALEGGKALK DVKLELHDAK GKLLAEASSD GDGHAQLPID AKADTLIATQ GVHTTLLRLS
GSALDLAEFD ITGPQNNPLQ FFIFGPRDLY RPGETVLLNG LLRDQDGKPV KAQPVNVEVR
RPDEQVSRKF VWEADANGLF QYQLQLSGEA PTGRWQLLLD LGGGRKQVYE FLVEDFLPER
LALELKGSAT PLSPEQTAHI QVNGRYLYGA PAAGNRLSGQ AYLRPMREAV PALPGYQFGS
VSESDLSQDL ELDEVTLDQA GKASLDIESR WAEARSPLQL TVQASLQESG GRPITRRFEQ
PIWPAERLPG LRGLFDGEET DSDAPVQFEI LVADREGNKL AADELKVRLI RERRDYYWNY
SQDDGWSYNF NEKFLTQSEE VVSVKAGSTT KLSFPVEWGP YRVEVEDPQT GIVSSERFWA
GYRAQDNAEG GAVRPDQVKL ALDKPAYSDG ATAQVTVTPP AAGSGYLMVE SADGPLWWQA
IEVPAEGKTF DIRLDPKWAR HDLYVSALVI RPGERKANAT PKRAVGVLHL PLQRGERKLA
LTLQAPEKMR PKQPLSVKLK AVNADGSVPK QVHVLFSAVD VGILNITDFK TPDPFASLFG
RKAYGADQLD IYGQLIEAGQ GRLASLAFGG DAAMAKGGKR PNTTVTIVAQ QSLPVTLDDK
GEGVATVDIP DFNGELRLMA QAWTDEHFGV AEGKTVVAAP LIAELSAPRF LAGGDRTRLA
LDLANLSGRA QQLTVHVRSE GQLSLTGSTE QQISLAEGQR QTLMIPVQAE GGLGQGKVLV
QVSGLELPGE AAKPFSREWT LGVRPAYPAL LKHFRVALKD QPWSLPEQEL AAFEPAGLEA
TLALSSRPPL NIAEQIRALE AYPYGCAEQT TSGLYPSLYA DAASLKRLGI KGEAADVRKR
KIEAGIEHLL GMQRYNGSFG LWSADSEEEY WLTAYVTDFL QRARDQGYGV PAKALKKANE
RLLRYLQERN LIEVEASDNV EHTRFAVQAY AALVLARNQQ APLGALRSLF ERRADVRSGL
PLVQLAVALE QMGDKPRAQE ALQAGLAVSR SKGWMADYGS PLRDQALILA LLEENKLAGN
QVEQRLFALS DELAANNWLS TQERNALFLA GRGLLGKPEG QWQARLDSAG DMRELNNQDA
GLKLEGAMLA SPLTVQNQSS DTLYQQLTLS GYPRQAPAPV SNGLEIRREY LGLNGQPLNL
GNLRSGDLVL VHVALKAKQY VPDALVVDLL PAGLELENQN LAQSAASLDN ASSAVKEWRE
SMQNANLVHQ EFRDDRYVAA VKLESYGTTH LLYLARAVTP GSYRIPPAQV ESMYRPNLQA
VGESQGELVV KPR
//
