ID A0A2D0KM76_9GAMM Unreviewed; 1686 AA.
AC A0A2D0KM76;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=Xsto_02950 {ECO:0000313|EMBL:PHM64544.1};
OS Xenorhabdus stockiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM64544.1, ECO:0000313|Proteomes:UP000222366};
RN [1] {ECO:0000313|EMBL:PHM64544.1, ECO:0000313|Proteomes:UP000222366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM64544.1,
RC ECO:0000313|Proteomes:UP000222366};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
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:PHM64544.1}.
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DR EMBL; NJAJ01000028; PHM64544.1; -; Genomic_DNA.
DR Proteomes; UP000222366; 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; 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.
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}.
FT DOMAIN 789..938
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1002..1091
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 39..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1686 AA; 188315 MW; 77B106A3606E0C05 CRC64;
MCQHQLRQWA TRKKRTITSM VVTLFAFFAL GILSGCDQSQ DNEKSIKPET SAIPAPSEIT
DTASRGSHSP VTQSPAAQSL PSQSLEEQYA GKDVTILDAS EVQLDGASAM VVTFSVPLNP
NQNFAQRVHL VDVKSGKLDG AWELSDNQME LRLRHLPPKR QLILTVDDGL QGINGRSLFN
VYEKKFQTAS IQPAVGFASK GVLLPSKLAE GLPVLALNVD RVDVNFFRIK EASLPMFIAH
GRYLRGITSW DSERLLENAD LVYTGRFDLN PTPNTREKLL LPLHDIKELQ KSGAYLAVMQ
QAGKYAYTNP AILFTRSDIG VSMHSYLNQI DVFAQSLEQG SGLKGVEVRV LDINGQLLAK
NTTDSNGHAT LEKSSKAALL LATQGEQVSM IDLSSPALDL SEFDIGGEQG YSRQFFVFGP
RDLYRSGETL IVNGLLRDAD GRLLKPQPVK VDILKADNQV ARSFVWQPEN GLYQYRYSIP
QSAETGMWSL RLDLGDNTPR YYKFNVEDFM PERMALEIKG NTDSRPIQKN ESVNFSIMGR
YLYGAPATEN RLQGQLFMRP DRDAVAKLSG YEFGSSKEEE LSRTLDEFDL ALNSEGKTDI
VVSEDNWKYV SSPVSILVQA SLLEAGGRPV TRHAEQAVWP AEKLVGIRPL FNKKSNYNYY
TDRYESRYNV NENSLAEFDV VYADADGKKY ATNDLRARLI YERRDYYWRW SDDGGWDSGY
DQKDLMMVDE PVQIVEEGTA KISFPVKWGS YRIEVVNQKN QLITSLNFWA GYSWQDNTEG
TGAVRPDQVK LSLDKPAYKP GDKVRLHIAA PQAGKGYLLL ESSDGPLWWQ EINVPAQGLD
IEVPINQSWA RHDLYLTAVV VRPGDKSRQA TSKRAIGVLH LPLMDEGRKL DLTLSAPDKV
RPNQDLSVKI KVTSQKGREL PKQVYVLLSA VDSGVLSITD FKTPDPYEAF FGRKRYSVDQ
YDVYGHLIES EGRKANLRFG GDVGEGEPER GGKKPLTVVN ILAEQAKPIS LNADGEGVIT
LPIPDFNGEL RLMAQAWSDD EFGNSERKVT VAAPVVAQMS LPRFMAGGDQ SQLALDLTNL
TEQPQKLTLN FATTGLIKLQ GSANNTITLE TGKRVTIQIP VKADYGFGQG EIFLTVDGLK
VSNEIQQYKN SWKIGVRPAY PAVTRQFADV IRQDEEWLLP PDAITGLAPE TLEGQLLLTS
RPPLQIARYI RELYAYPYGC LEQTISGLYP SLYSNEAELK KLGIKTQTDE SRRAAIDAGI
THLLSMQRHD GSFSLWDRHG EEEFWLTAYA ADFLFRANQQ GYSIPVDALK NANNRLLRYL
QDKNTINDRY SGSHSATQFS VRAYAGLVLA SQQKAPLSSL RQLYDQREQA DSGLSLVQLG
IALRMMGDDN RGNEAIHSGV SKSRQPGYGL LDYGSTIRDD ALIVALLTEN NILQKERDKK
LLALSNELSS RKYFSTQESN ALYLAGRYFI DASEQPWKAV INRQIPPINR DTALNNALSA
KQLLHGIEIS NRGDNSLYSR LNVVGYPLQK PEPYSNILNI KRTYLDLAGK TYTPDRLNSG
ELMIVKLEIS TTQPVSDALV VDLLPAGLEL ENQNLAYSSA SLSESATDLQ DMIYRMQRAN
IRHMEYRDDR FVAAVSVEPY QPVTLLYLAR AVAPGVYQIP APQVESMYVP YWRAVGETGE
KLEVVR
//
