ID A0A0A7LNT1_9BACT Unreviewed; 1847 AA.
AC A0A0A7LNT1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN ORFNames=PK28_05330 {ECO:0000313|EMBL:AIZ65031.1};
OS Hymenobacter sp. DG25B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1385664 {ECO:0000313|EMBL:AIZ65031.1, ECO:0000313|Proteomes:UP000030789};
RN [1] {ECO:0000313|EMBL:AIZ65031.1, ECO:0000313|Proteomes:UP000030789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG25B {ECO:0000313|EMBL:AIZ65031.1,
RC ECO:0000313|Proteomes:UP000030789};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter radioresistens genome sequence.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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; CP010054; AIZ65031.1; -; Genomic_DNA.
DR STRING; 1385664.PK28_05330; -.
DR KEGG; hyd:PK28_05330; -.
DR HOGENOM; CLU_000965_2_1_10; -.
DR Proteomes; UP000030789; Chromosome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd02891; A2M_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR Gene3D; 2.60.40.3710; -; 1.
DR InterPro; IPR011625; A2M_N_BRD.
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; PF07703; A2M_BRD; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000030789};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1847
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002029615"
FT DOMAIN 952..1090
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1150..1239
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1847 AA; 203272 MW; 94713C50527ED123 CRC64;
MRQTLSRLSL LVLLALFGAC SKTGSNAGSD ANGEEIDPYQ NLVFQFDEDV VGKEQQDRWD
TIQYVQFEPA VRGKFKWSSE RELIFSPLTP FRPSTAFTAK LQTEALPTEK RNIRLPENRE
KFHTPYLQLD PPQAFWGRSA RAAGTAEMRV ELPFNYPVRP TDVKPLLRLT QDGQPVAFDV
PNAEPGQNVS VHLTQQVHAG SPLTVALAPG LHAVGSDQPT ARDYSAEVTV PDPQALEVRS
ITGNMETAEA TITILTNQPV SQQELQSSLT VTPQAPFQIE ELESGVALKG GFEVGKSYQI
TLRHGLRGAL GGQLAETTTQ TVSFSAERPS IQFAAADKAM YLDALGTRNL GVRINEVAKV
KVTIAKVYAN NIQQLLRGGT QYGYPEYDET ESNQQEEGEY VDRSFQYYDV ENLGNVLTER
TYTVNGLPKE QGLRLLNLSL KDLEFSGGMK GLYIVKVQDT ERQWLQVSKL VAVSDIGLIV
KQGKAGSTLV FANSIRNARP LAGVQVRYVS TNNQVIGTGI TNREGVAKFD STAANSRFRL
GMIVAQKEAD FTFLDLTRSR VETSRFEVGG LQSNAARYQA FLYGDRDLYR PGDTIRTNTI
IRTEGWKNPP AKLPVKIRLL LPTGKEYASL RKQLTPEGTF EASFIMPPSV MTGIYTLEVL
TGNDVLLTSR KISVEEFIPD RMKVTVKADR AVAKPGQTVS ALITAQNLFG PPAADRKFEV
EFSLKEKSFA PKNYPDYTFA INSGEKQRGS YGEQESTPIS ARFEKTMREG TTDANGRGTA
TYEVPDYTDL GTLEGAAFAT VFDETGRPVN RLATFEVQTQ PVMFGVKNLD ELVATRTQLP
VRLVALTPAG APTTAQARVQ VVRLLWETVI ERQGGRYIYN SQKREQVVLS RTVMVPSGGA
DAGLNFAPNY SGEYEIRVSR PGASTYVARR VYAYGFGDTQ SNSFEVNNEG EVTIEADKAK
YQPGETAHLL LKTPFPGRVL VTVERDRVLD HFYVNTDEKS ARVSIPIRAG HVPNVYVTAT
AIREIKDNRL PLTVARGFVP LMVEKPEARL KVAIKAPAQS RSQTWQTIEV STAPKAKVTL
AVVDEGILQM KDYRTPDPYG YFYQKRALEV QAYDVYTFLL PELGTSSTGG DVGDLARRTT
PVPNRRVKLV AKWSGVLTAD ASGKVRYKVR VPQFSGALRV MAVAYKDDAF GSAEHTMRVA
DPVVISTALP RFLSPGDTID VPVTLTNTTE KEMNVIATLK YNSLLRIQEL KNTYVADKRS
GEVIKWTPIP NNIPQTLKPN SEGRVVFHIV ANGIGAGSVT VSVKPTDSKE TFTETIEIPV
RPASPLQKRT GAGVVAGGAS QQLNLKTDFL PSSLRSQLVV SRSPMTEFAR DLRYLLQYPY
GCLEQTVSAA FPQLYYGDLA ATLGQKTGIS KAVMFNPNYH VQEAIRKVEA QQMYNGSLSY
WPGGDFDNWW STAYVAHFLL EARQAGFAVN EPVLDRVLRY LQARVRKREM ETYNVILTSG
QIQPLAQAKR ETAYSLYVLA LAGRPDATGL NYYKANRQLL TSDARYLLAA AFALSGNQRG
YQSTVPSRYN AAPTAASREL GNSFSSPIRD QALVLNALLA ADPGNPQIPG MARELSRQVK
RASWLNTQER AFSLLALGKL ARKNAGSTVT ASLLADGKAI GNFSGKDLTV TNVANRQLAL
RTQGQGSLYY FWETEGISPG GQVLEEDAYL QVRRTFLTRT GQPVGAPAFR QNDLVVVKIT
LQAPGAAGEI KNVAITDLLP AGLEIENPRI GAVRELAWAT DAAQPDYLDV RDDRINLFTT
ATAQPKSFYY LCRAVSKGTF KLGPVSADAM YNAEYHSYSG AGVVRVR
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