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
//