ID Q8XA93_ECO57 Unreviewed; 1653 AA.
AC Q8XA93; A0A0H3JHI3; A0A6M0JH99; Q7ABM1;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN Name=yfhM {ECO:0000313|EMBL:BAB36809.1};
GN ORFNames=ECs_3386 {ECO:0000313|EMBL:BAB36809.1};
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB36809.1, ECO:0000313|Proteomes:UP000000558};
RN [1] {ECO:0000313|EMBL:BAB36809.1, ECO:0000313|Proteomes:UP000000558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC {ECO:0000313|Proteomes:UP000000558};
RX PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; BA000007; BAB36809.1; -; Genomic_DNA.
DR RefSeq; NP_311413.1; NC_002695.1.
DR RefSeq; WP_000736260.1; NZ_VOAI01000001.1.
DR SMR; Q8XA93; -.
DR STRING; 155864.Z3787; -.
DR MEROPS; I39.008; -.
DR GeneID; 912952; -.
DR KEGG; ecs:ECs_3386; -.
DR PATRIC; fig|386585.9.peg.3537; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000965_1_0_6; -.
DR OMA; LDRYPYG; -.
DR Proteomes; UP000000558; 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:UP000000558};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1653
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035184832"
FT DOMAIN 758..906
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 968..1057
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1653 AA; 181416 MW; E4C84A54ECDAC25A CRC64;
MKKLRVAACM LMLALAGCDN NDNAPTAVKK DAPSEVTKAA SSENASSAKL SAPERQKLAQ
QSAGKALTLL DLSEVQLDGA ATLVLTFSIP LDPDQDFSRV IHVVDKKSGK VDGAWELSDN
LKELRLRHLE PKRDLIVTIG KEVKALNNAT FSKDYEKTIT TRDIQPSVGF ASRGSLLPGK
VVEGLPVMAL NVNNVDVNFF RVKPESLPAF ISQWEYRNSL ANWQSDKLLQ MADLVYTGRF
DLNPARNTRE KLLLPLGDIK PLQQAGVYLA VMNQAGRYDY SNPATLFTLS DIGVSAHRYH
NRLDIFTQSL ENGAAQQGIE VSLLNEKGQT LTQATSDAQG HVQLENDKNA ALLLARKDGQ
TTLLDLKLPA LDLAEFNIAG APGYSKQFFM FGPRDLYRPG ETVILNGLLR DADGKALPNQ
PIKLDVIKPD GQVLRSVVSQ PENGLYHFTW PLDSNAATGM WHIRANTGDN QYRMWDFHVE
DFMPERMALN LTGEKTPLTP NDEVKFSVVG YYLYGAPANG NTLQGQLFLR PLREAVSALP
GFEFGDIAAE NLSRTLDEVQ LTLDDKGRGE VSTESQWKET HSPLQVIFQG SLLESGGRPV
TRRAEQAIWP ADALPGIRPQ FASKSVYDYR TDSTVKQPIV DEGSNAAFDI VYSDAQGVKK
AVSGLQVRLI RERRDYYWNW SEDEGWQSQF DQKDLIENEQ TLDLKADETG KVSFPVEWGA
YRLEVKAPNE AVSSVRFWAG YSWQDNSDGS GAVRPDRVTL KLDKAGYRPG DTIKLHIAAP
TAGKGYAMVE SSEGPLWWQE IDVPAQGLDL TIPVDKTWNR HDLYLSTLVV RPGDKSRSAT
PKRAVGVLHL PLGDENRRLD LALETPAKMR PNQPLTVKIK ASTKNGEKPK QVNVLVSAVD
SGVLNITDYV TPDPWQAFFG QKRYGADIYD IYGQVIEGQG RLAALRFGGD GDELKRGGKP
PVNHVNIVAQ QALPVTLNEQ GEGSVTLPIG DFNGELRVMA QAWTADEFGS NESKVIVAAP
VIAELNMPRF MASGDNSRLT LDITNLTDKP QKLNVALTAS GLLELVSDSP AAVELAPGVR
TTLFIPVRAL PGYGDGEIQA TISGLALPGE TVADQHKQWK IGVRPAFPAQ TVNYGTALQP
GETWAIPADG LQNFSPVTLE GQLLLSGKPP LNIARYIKEL KAYPYGCLEQ TASGLFPSLY
TNAAQLQALG IKGDSDEKRR ASVDIGISRL LQMQRDNGGF ALWDKNGDEE YWLTAYVMDF
LVRAGEQGYS VPTDAINRGN ERLLRYLQDP GMMSIPYADN LKASKFAVQS YAALVLARQQ
KAPLGALREI WEHRADAASG LPLLQLGVAL KTMGDATRDE EAIALALKTP RNSDERIWLG
DYGSPLRDNA LMLSLLEENK LLPDEQYSLL NTLSQQAFGE RWLSTQESNA LFLAARTIQD
LPGKWQAQTS FSAEPLTGEK AQNSNLNSDQ LATLQVTNSG EQPLWLRVDA SGYPQSAPLP
ANNVLQIERH ILGTDGKSKS LDSLRSGDLV LVWLQVKASN SVPDALVVDL LPAGLELENQ
NLANGSASLE QSGGEVQNLL NQMQQASIKH IEFRDDRFVA AVAVDEYQPV TLVYLARAVT
PGTYQVPQPM VESMYVPQWR ATGAAEDLLI VRP
//
