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Database: UniProt
Entry: H5UYB5_ATLHE
LinkDB: H5UYB5_ATLHE
Original site: H5UYB5_ATLHE 
ID   H5UYB5_ATLHE            Unreviewed;      1653 AA.
AC   H5UYB5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN   Name=yfhM {ECO:0000313|EMBL:GAB50896.1};
GN   ORFNames=EH105704_01_09080 {ECO:0000313|EMBL:GAB50896.1};
OS   Atlantibacter hermannii NBRC 105704.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Atlantibacter.
OX   NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB50896.1, ECO:0000313|Proteomes:UP000010297};
RN   [1] {ECO:0000313|EMBL:GAB50896.1, ECO:0000313|Proteomes:UP000010297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB50896.1,
RC   ECO:0000313|Proteomes:UP000010297};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL   Submitted (FEB-2012) 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:GAB50896.1}.
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DR   EMBL; BAFF01000001; GAB50896.1; -; Genomic_DNA.
DR   RefSeq; WP_002463678.1; NZ_BAFF01000001.1.
DR   eggNOG; COG2373; Bacteria.
DR   Proteomes; UP000010297; 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.
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:UP000010297};
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_5003600031"
FT   DOMAIN          758..907
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          969..1058
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          27..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1653 AA;  180221 MW;  DC216F8BC32B92CC CRC64;
     MIRARHAALA AALFAMFSLT GCDDVKSQAA GESTPAPAQK SQSAAVSAKP DSAKLAQLAG
     QSAGKPLTLI DASEVQLDGA ATLVLTFSIP LDPSQDFSRT VHLVDKKDGK VDGAWELAPN
     LKELRMRHLE PHRTLVASVD SELKALNEAT FGINWEKTIE TRDIAPSVGF ASRGSLLPTK
     VVQGLPVMAL NIDNVDVNFF RIKPESLPSF VSQWEYRSSL TNWESEKILQ MADLVYTGRF
     DLNPARNTRE KLLLPLGDIK PLQQPGVYLA VMNQAGRYNY SNAATLFTLS DVGVSLHRFH
     NRLDVFTQSL ENGAVQGNVE IQLLSEKGQP LAQAKTDGDG HATLETPKEA ALVLARSGDQ
     TTLLDLKLPA LDLSEFDIVG EAGYARQFFM FGPRDLYRPG ETVIFNGLLR DGDGKPVNDQ
     PIKLEVVKPD GQVARTEVVQ PHNGLYQFTW PLAASAATGN WHIRANIGDN QPRDWRFQVE
     DFMPERMALT LSPQKTPITP KDPLAIPVEG HYLYGAPASG NALQGQLFLR PLRDAVPALP
     GYEFGDITEE NLSRSLDEVQ LTLDEQGHSE VALDSQWQDA RSPLKVILQA SLLESGGRPI
     TRRAEQPVWP AVALPGIRPQ FASKAVYDYR SDTTVNQPMV DEGSLAGFDI VYTNAQGEKL
     AVNDLQVRLI RERRDYFWDW SESDGWQSQF DQKDLVEGEQ SLNLAAGETG KVSFPVDWGS
     YRLEVKGPND TVSSIRFWAG YSWQDNSDGS GSPRPDRVTL KLDKPAYQPG DTIKLHIAAP
     AAGKGYAMIE SSDGPLWWQA IDVPEGGMDL SIPVDKKWQR HDLYVSTLVV RPGDKSKSAT
     PKRAVGILHL PLGDENRRLA LTLDAPAKMR PDRNLDVKLK VKPNAQGTIP AKVNVLVSAV
     DSGVLNITDY RTPDPWQAFF GKKAYGADIY DIYGQVIEGQ GRLAALRFGG DGDELNRGGK
     PPVNHVTIVA QQALPVVLNE NGEGTVQLPI GDFNGELRVM AQAWTADSFG SSEAKVIVAA
     PLIAEISMPR FLAGGDESRL ALDVSNLTDS AQNLTVSLTA SGLVSLLENP ELKVSLKPGA
     RKTLFIPVRA HEGFGDGEIQ AQISGLNVPG ETFVPSQKQW KIGVRPAFPS QTVNSGVMLN
     PGESWQVPAS HIEGFSADTL EGRLLLSGRP PLNLARYISE LKAYPYGCLE QTTSGLFPSL
     YTSAAQLKAL GIAGESDKQR RAAIDLGISR LLEMQREDGG FSLWDKTGPE EYWGTAYVTD
     FLVRATEQGY SVPADALERA NNRLLRYLQD PGLMALRYSD NSAASKFAVQ AYAGLVLARQ
     QKAPLGALRE LWNRHNAAVS GLPLVQLGVA LKLMGDATRS QDAINAGIST TRNNRTEWIG
     DYGSELRDNA LILNLLEENK LLTQQQAGLL QKLSDQAFGQ NWLSTQESNA LFLAGRAWQN
     QPASWQVESS LSGEPLQGDK AQAFNLNADK LASLHLTNTS DSPVWVRLDS VGYPQSAPQE
     SGNVLKIQRH FLASDGTAKS LDNLRSGELV MVWLDVYASK TVPDALVVDL LPAGLELENQ
     NLANASASLG ESSGTVTDLV SRMQQQDIQH MEFRDDRFVA ALPVNAGEHA TLVYLARAVT
     PGRYTVPVPQ VESMYVPAWR ATGRSEGTLT IAP
//
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