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
//