ID   A0A0Q4YBA4_9BURK        Unreviewed;      1982 AA.
AC   A0A0Q4YBA4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Alpha-2-macroglobulin {ECO:0000313|EMBL:KQP17650.1};
GN   ORFNames=ASF43_07105 {ECO:0000313|EMBL:KQP17650.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP17650.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP17650.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP17650.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP17650.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP17650.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KQP17650.1}.
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DR   EMBL; LMMV01000012; KQP17650.1; -; Genomic_DNA.
DR   RefSeq; WP_056181128.1; NZ_LMMV01000012.1.
DR   STRING; 1736316.ASF43_07105; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000051560; Unassembled WGS sequence.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR021868; Alpha_2_Macroglob_MG3.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
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; PF01835; MG2; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01359; A2M_N_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1982
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006240697"
FT   DOMAIN          1032..1215
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1273..1363
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          818..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..840
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1982 AA;  213457 MW;  5D68229F4F9845E5 CRC64;
     MAFPSFFLTA VLALTAASAA QALQITNASP QGEVAQVRQV VLRFDADAVR SGDAAAKPPA
     TVSCSDNAAG RGTGRWNSAR EWVWQFQDDL PPGVRCTIAA APGFQSPQNQ ALTGHTSFAF
     NTGGPFVRNT RPYGGAIDEE QYFVLRLNGP ATLASVQANV WCQVEGLGER VPVKLVEGAE
     RAALLKARRL DEEAAKAPLA VQTLACNRRL PPSAEVQLVF GTGVATPSGI ANNVEKRFNF
     KVREPFTASF SCERENANAA CLPIRPLRLQ FNAPVPRALA EAIRLKTGSQ SVAPTFEAQD
     KDAQVTGVQF APPFAESANH SIVLPANFKD DAGRALANAD SYPLQVATGA MPPLAKFAAA
     PFGIVERFAE PDSPPMLPVT LRNVEAQLPL AAKAIAADAR VANLRPESDA EILAWFRKLQ
     RYDNATVLRK RAAAELTTPL PRIVDSDQRE WVQTRMLSLL AGQAGVRAMD LPKPATSDPR
     LFEVVGIPLT PGFHVLEISS KRLGAALLDE RYGPQRTMVV RSSALVTNLG VHFKLGRENA
     LAWVTTLDKG QPVAGARVAV SDCRGKPVAS GTTDAQGVVQ LAGLSPQPPA CNDRDDDYTA
     PSWFVTARAR DAKGVDDMAF TFSDWNRGIE PWRFDVPTSQ DPNPDLRAHT IFDRTLLRAG
     ETVAMKHLLR TETAKGLALP EQFPTRLQIT HVGSGQQFTQ PLAWRKTATG GQSAESQFAL
     PPAAKLGAYE VALLQGGERD ARSLPSGQFR VEEFRLPVLE GRIAPADARP LVKPESVPTN
     VQVNYVSGGG AANLPVRVSA LLRDRALHFD GFDAFSFTPP RDRAANPSNE DEEEPEATSG
     PRVIADKLAL NLDASGAGKL TIDKIPAAPR AQELLLEATY ADPNGEVQTL RSTATVWPAG
     VVAGIKTEGW VSSAQKIRFQ ALALDLAGKP QAGVALEVTA IARIVTTSRK RMVGGFYTYD
     NKSEGKDLGS VCSGKSDARG LLLCEAKLAE AGEVELVVTA KDAAGLAVQA ASSVYVTRQG
     ELWFGGENHD RIDLLPEKKD YAPGETARLQ LRMPFRYATA LVTVEREGVL SHRVVQLNGQ
     DPTLELKIEE GWGPNVYVSA LVLRGRLREV PWYSLFTWGY KAPREWWTAF WHEGREYVAP
     SALVDLSKPA FRLGVAELRV GTRAHQIDVK VAADQPTYQV RGQARVTIQA TLPDGKPAAN
     AEVALAAVDQ ALLELMPNDS WNLLAAMLQR RAWGVETSTA QMEIIGRRHY GRKAVPAGGG
     GGRGATRELL DTLLLWNPRV VLDANGQAVV TVPLNDALTT FKIVAVADAG TALFGTGQAS
     IRTTQDLQII SGLPPLVRED DKFRAQLTLR NTTTKAMKVD VAPRATLLTL PAQTVDIPAG
     EAREVVWDVT APAQLAQTRA EAILWEIEAK DQASGARDAL KASQRILPAV PLTVQQATLV
     QLDGPFSLPV QPPADALANE GRARGGLQLA LQPRLAEGLP GVRDWFANYP YSCLEQQTSK
     AIGLRDAKRW QGVVAQMPTY LDGDGLAHYF PPRDGSANRG SDTLTAYLLA ATHEASTLQP
     AFALPEALRT QMENGLVAFV EGRLQREFWS PRADLDVRKL AALEALSRSG RAQGRMLASI
     TVAPNQWPTH AVIDWLSVLK RVADAPQREQ RLAEAQQVLR ARIATSGTKM VFSTERDDQW
     WWLMVNGDVN AARLLLAVMD DAAWKDDMGR LAAGFIARQQ RGAWQTTTAN LWGGLALEKF
     SAKFETTPVA GVTTARLGDA AASVDWAKVE RVQSTDASGA PHQAGGFGAP AAPGALRGNT
     AFLPWPTGGM GTVEVAQQGT GKPWLTLQSL AAVPLKAPFD AGYRIAKTIT PVEQAVAGRY
     SRGDVLRVTL EVTAASDMTW VVLSDPIPGG ATILGSGLGR DSAIATQGER QGAAGWPAFE
     ERSFEAYRGY YDFLPRGTMK AVYTLRLNNV GDFALPPTRV EALYAPEMFG ALPNARVKVE
     AR
//