ID M5E929_9GAMM Unreviewed; 1654 AA.
AC M5E929;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=TOL_3475 {ECO:0000313|EMBL:CCU73861.1};
OS Thalassolituus oleivorans MIL-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Thalassolituus.
OX NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU73861.1, ECO:0000313|Proteomes:UP000011866};
RN [1] {ECO:0000313|EMBL:CCU73861.1, ECO:0000313|Proteomes:UP000011866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIL-1 {ECO:0000313|EMBL:CCU73861.1,
RC ECO:0000313|Proteomes:UP000011866};
RX PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA Yakimov M.M., Teeling H., Golyshina O.V.;
RT "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL Genome Announc. 1:1-3(2013).
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; HF680312; CCU73861.1; -; Genomic_DNA.
DR RefSeq; WP_015488564.1; NC_020888.1.
DR STRING; 187493.CN03_17240; -.
DR KEGG; tol:TOL_3475; -.
DR PATRIC; fig|1298593.3.peg.3357; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000965_1_0_6; -.
DR Proteomes; UP000011866; 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; 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; 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:UP000011866}.
FT DOMAIN 762..909
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 973..1060
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1654 AA; 183060 MW; 24DFFB99024B3DC9 CRC64;
MLNLRSLSFA LLIPALLSLY GCQDDKSEAT AGQTSTASPN AMATDDTSGP INEPIDPSLY
QGMPLEVALI AEGTYDDGTV LAVTFSAPLD PKRDFQSFLR VNRLIKNSSD QASEAEHVAE
VISGQWILAP DARHAYFTQI DPDTRYRVTV QPGLVGLTGV SLMQPHTADI DIGSIAPSVS
FASSGHFLPL GLHSGLPIYA LNVAEANVSF FRVEPGKEKA MMNWIGNSVS RPYYWMDTIP
TFASLIHEGR FTLTTERNKR RQMNLPIQDV AALQQAGVYV AVMSRPGQYD SQFAITYFMV
TDLGVHVRQY KNSFDIYISD LNSPSPIAGA DVRIYNDNGS VAFDASSSAS GVVNVAQLPK
HGQLLVVTKG DATSILPLST AALDLSEFHL SSRDYREEEL FIYTPRDIYR GGDEVVLSAL
LRNDDGKPLA ARPLQASLFR PDGQKIKTFA WQPSAPGYYE WRYALGDDAQ TGNWRLTVEG
ASAAQSFQFK VEDFMPERLK ITYNEGKPAK LLAKSDDMSV AVLGEYLYGA PASGNKFSAA
IRIRPEPHPF AELADFSFGN AGTDTDRINF DYDDKELNKD GKLDLVVASR WQNTATPLKV
TLTGSLFESG GRPVVRRYSA NVIPADTMIG VRPLFKDRAK ARTLAQFELI RTNQAQEKLA
AAELTVRLIN RTHRYHWRFS SSDGWYMDDT AQEFTELTLT SAITAGETTN IEFPVDWGDY
RIEVSDPDSN ILTSYEFSAG ENWYRRWSQA SDAEQGAAPD QVVLALDRSG YSAGDVAKLR
IVPPAAGHTL VMVESDHLLW MRRVESPAEG TTVDIPISAD WARHDLHITA LHLQSADEQE
RITPTRSVGI IHLPLDRSAR ELTVTLPEDA SWLPNTEVSV AVDVADKQGQ PIQQAWVTLA
AVDVGILSIT DFKTPDPFKY FFEPRAYRVD MFDMYSRLIS LNRNPLARQR FGGDAPALSR
GGDKARAEVQ IVSLFSGLVT VTDGKANISF TLPDFNGRVR LMAIAFDDTR FGMAEQEVTI
AAPVVTQLSM PRFLAMGDLS QVALDVSNLS GKDQTFKLQL SSSGAAVGNS IQRDLVLSDG
ARTTIILPVE GSYPAGAIDI AMQLTDESGE VLQRHWQLNT RAANPAKTEQ YNRLLNAGES
YHLSPAAMGN WLPETLGVSV SINNQINLNP KNQLRELFHY PYGCLEQSIS STYPWLYISE
KKAAKIIQPL PQGQREKSLI EGLRRVVTRQ KVNGGYGLWS SNDTYEQHWL TAYAGDFLTD
AIDQGVDVPK DVMQQTLNRL KEYVRGRGTM QERWSGRPDL YRPTYTAYAA YVLSRHKRAP
LADIRRLAQE RPKDLSSLPL LHLALAADAQ GDKALAAELL TAMKNAPRES NFYLGDYGSD
IRDDAKIVTL LLTHNIEQSY AMTLAASLAE SVRKHRYLST QERNALFMAA LQLAQTKGES
WQARLELAGL QRTLQQVGEF AEVHYGPELS DGLAIVNSGD KPILAVVQTQ GISNTPPKPE
ANGSTLERRY FSLAGEPIFP VDGALNMKVG DMMLVQVELT AQKRHPDMLL VDLLPAGLEL
ENQNLSSSKK LDELSLQGKP LSEWQNAKIV HEEFRDDRYV AAVDLNHYRT NRLYYLVRAV
TPGHYQVPAP LLEDMYNPSI RAIGKTPDIL NIEP
//
