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Database: UniProt
Entry: A0A0R0D7Z0_9GAMM
LinkDB: A0A0R0D7Z0_9GAMM
Original site: A0A0R0D7Z0_9GAMM 
ID   A0A0R0D7Z0_9GAMM        Unreviewed;      1644 AA.
AC   A0A0R0D7Z0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN   ORFNames=ABB28_11375 {ECO:0000313|EMBL:KRG73336.1};
OS   Stenotrophomonas chelatiphaga.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=517011 {ECO:0000313|EMBL:KRG73336.1, ECO:0000313|Proteomes:UP000051386};
RN   [1] {ECO:0000313|EMBL:KRG73336.1, ECO:0000313|Proteomes:UP000051386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21508 {ECO:0000313|EMBL:KRG73336.1,
RC   ECO:0000313|Proteomes:UP000051386};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRG73336.1}.
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DR   EMBL; LDJK01000049; KRG73336.1; -; Genomic_DNA.
DR   RefSeq; WP_057508730.1; NZ_LDJK01000049.1.
DR   PATRIC; fig|517011.3.peg.1988; -.
DR   Proteomes; UP000051386; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1644
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006395250"
FT   DOMAIN          750..893
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          957..1046
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1644 AA;  179096 MW;  ACC906DF143EB022 CRC64;
     MTGPQRLRKW GWAAALMAGS LLAGITGCNR NDSGQLPAAS GEAITAKAEQ VTEFTLLRAY
     PDQKNDGLSL ALEFSRPLVG TQDFDALVRF EEKVGTDDSS WTLSDDGKTL RYPFVEAAKE
     YSLVVSADLL AADGSRLGKE LRQKVFSGEL TPVAGFASQG SVLPARDSRG LPVVSVNVPE
     VDVEFLRVRE KELPTFFSQY QRGGRRGSWE LDSDYSERTP ISRLAEPVYV NRFILGGKQN
     ERVLTYLPTQ DIKELQEPGL YFAVLKRTGA FDGEFDTAFF SVSDIGLHTR AYKDKLFVHT
     ASLKDGAPLK KVDVRVLDGK GEVVLRGSTD GNGNALLDYT LDASHVLVAG SGKDTSFLPF
     NQPALDLSEF AVAGRDNAWF DVFAWSGRDL YRPGETVRLS ALLRDNDGKP VAPGKDAKAR
     QPVFLRLKQP DGKIFRETQL QPGEQGYFNF EQLIPADAPT GRWQVEFRTD PASKEAIQGM
     TLRIEEFLPE RMKLDLDSAQ KSLKPGDALR LQANGAYLYG APADGNRFTA RLAVAVEQTP
     VEGLPGYFFG DPTVSLPREA KDVVDTTLPA DGMLKQDVDL PEEAAKAKTP VAVVLSGSLY
     ETGGRTVNRT LKRVMWPAAA LVGVRPLFNP DDGADANGTA RFELMRVDAA GKPQPAKGLK
     VTLVRELRDY HWAFNDNRWD YDFTRRFENK DTRTVDAGTS AVAFDVPVEW GEYRVDVFDP
     ATGLTSRYPF RAGWSWGDDN RGLDARPDKV KLGLDKTGYK AGDTLEVTVT PPHAGRGLLM
     VETDRMIYVQ DIDAKPGSTF RIPVTADWER HDVYITALVF RGGSAPSKVT PARAVGVVHV
     PMDRKARTVA VGLVAPKQMR PEQDLPVTVS VPQLAGKVAH VTVSAVDVGI LNITRFPVPD
     AAAHFFAQRR LGIDAYDIYS RVIESFDGSS GKLKFGGDMA LAALPQAKRP TARVQTVDLF
     TGPVKLDAKG NARVRLKVPD FNGTLRVSAL VYADESYGKR DVETVVRAPL LAEASMPRVL
     APGDRSTVTL DVQNFTGKPG QFNVRVETEG PLSLAEGTRS VQLAADAKST LSFPLSAREG
     HSVAKVRVRV DGNGFKADRR YDLPVRAAWP QVLRSQVRTL DPLAAVSLDG SLMDGLMPES
     VTARLLVSPL PPIPFASALQ GALNYPYGCA EQTTSKGYAA LILDQATSTM LGADGLDAKV
     RRERMEGAFG RLASMQVANG NFSMWGDDGY VNPWLTPYIT EFLLDARDAG FAVPENVLQK
     ALNRLSEDLL SGGNQFYGQD RRDNLKFANQ AYSGYVLARV NRAPLGTLRT LYDNERAKAI
     GGLPLVHLGV ALSLQGDRKR GEAAIAAGFA KPSSERPSYF GDYGSAIRDD ALMIALTHEH
     NLAKPAWDAR SVDLGRELDS RRNRGWMWLS TQEQVAIARL GKALAANQKK LVAGELVIGA
     QTESIGERRL FGRGFDAAQL LSGVRFAPTG EPPMFASIDV AGIPRTAPAP DNSVIGVERS
     WFGTDGKPWT PRPLKEGEAL IVRVTVTPDS SMPDALLTDL LPAGLEIENF NLGDAKQWAD
     VVVDGIGISA RGDAADVKHE EFRDDRYVAA LNLSRGSKAT LFYLVRAVTP GTYTVPPSLV
     EDMYRPQLRG VGRSNPSTIT VVQP
//
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