ID W1IU65_9GAMM Unreviewed; 1698 AA.
AC W1IU65;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN Name=yfhM {ECO:0000313|EMBL:CDL81161.1};
GN ORFNames=XSR1_110044 {ECO:0000313|EMBL:CDL81161.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL81161.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL81161.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL81161.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-2013) 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:CDL81161.1}.
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DR EMBL; CBXF010000013; CDL81161.1; -; Genomic_DNA.
DR RefSeq; WP_038234542.1; NZ_NIBV01000003.1.
DR STRING; 1427518.XSR1_110044; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000019202; 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 Lipoprotein {ECO:0000313|EMBL:CDL81161.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Protease inhibitor {ECO:0000256|PIRNR:PIRNR038980};
KW Reference proteome {ECO:0000313|Proteomes:UP000019202};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1698
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004804036"
FT DOMAIN 800..949
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1013..1102
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 39..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1698 AA; 189783 MW; 8CED6C1CE0C15A40 CRC64;
MYQCQFWQRS ARKKRYLAVM LISLFTVFML SGCDQSENTE KTELAEKNNI SSSQQSPQNS
QSIESATEKQ SQSVNQNGEE AISEGSVTKT QVSQSPEQRY AGKDVTIVDA SELQLDGAST
MVVTFSVPLE PDQDFSQKMH LIDVKSGKLD GGWELSNNQM ELRLRHLPPA RELQLTIDEG
IKGINGRRLA SVYKNKFVTR PITPTVGFAS KGLILPSKIA EGLPVLALNV NSIDVNFFRI
KDEALPSFIS SWQSRDSMFY WESKELLEET ELVYTGRFDL NPAANTREKL LLPISNIKEL
QKEGVYLAVM QQAGKYTYSN PITLFTLSDI GVSVHSYLNR MDVFAQSLEE GTSLKGVEIR
LLDIKGQLLS KATTDNDGHV SLEKNDKAKL LLASQNGRTS IINLHYPALD LSEFDIGGPE
GYSKQFFVFG PRDIYRPGET LIVNGLLRDA DGRPLKSQPV KVDVLKAGDQ VVRSFVWQAE
NELYQYRYPI PREAETGMWA LRFDLGDNAP RYYKFNVEDF MPERMALEIK GNIDDQPLLK
NEDVEFSVTG RYLYGAPAAE NRLQGQMFLR PVREAVATLP GYEFGVADES DVYRALDEFD
VTLDSEGKTV LSIDSENWES VKSPVKVVVQ ASLLESGGRP VTRRVEQAIW PAKQLVGVRP
LFNKKTIYDY RSGRDESRYN VDENSLAEFA IVYADAKGKK YAASELRARL VYERRDYYWR
WSDNDGWDSG YNQKDLVMAD EHIQIAENGI AKISFPVDWG SYRIEVINPE NQLVTSLNFW
AGYSWQDNTD GTGAVRPDQV KLSLDKPAYT LGDKVKLRMV APHEGKGYLL VESSDGPLWW
KEINVPEKGL DIEVPINQAW ARHDLYLTAV VVRPGDKSRQ ATPKRAIGVL HLPLTDEGRK
LNVALSAPDK IRPNQDLAVK IKAMPQKGKA LPKQVNVLLS AVDTGVLSIT NFKTPDPYDA
FFGRKRYGVD QYDVYGRLIE AEGRQANLRF GGDADDDTYD RGGKKPLTEV NIIAEQAKPI
MLDVNGEGEI ILPIPDFNGE LRLMAQAWSD EEFGHGERKI TVAAPIVTQM SLPRFMAGGD
QSQLSLDLTN LTEHPQALTL NVTAEGLIKL QNLTSKKLIL EKGKRTTVHI PVQADHGFGQ
GEVFLTIDGL NLPDENLEQY KNSWKIGVRP AHPAETLQFA EVLHKDKNWQ LPPTAISGLA
PETLEGQLML TSRPPLQISR YIRELYAYPY GCLEQTVSGL YPSLYSNEAE LKKLGINTQD
DEKRRKAIEA GITHLLSMQR HDGSFSLWDR NGDEEFWLTA YATDFLFRAT QQGYSVPVDS
LKEANNRLLR YLQDKTIISD RYMGSHPATQ FSVQAYAGLV LAGQQKAPLS GLRQLYERHA
QAESGLSLVQ LGIALKMMGD NTRGDEAVHL GVNKSRVSGY GLGDYGSTIR DNALIVALLA
EHNMLTKERD GKLLNLSNEL TTRSYFSTQE SNALYLAGRY FIGTTEQPWE ALINQQEPFI
KRDSALTETL STDQIAKGIA IKNRGDSILY SRLNIVGYPL KAPAPSSNVL SINRTYFDLE
GNPAYIGQMK SGDMVVVKLE VRATQTVPDA LVVDLLPAGL EIENQNLANS SASLSESATG
LQDLIEEMQQ ADIRHIEYRD DRFVAAVAVP SYKSVTLLYL ARAVAPGVYQ IPAPQVESMY
VPNWRAVGAT NSKLEVVR
//
