ID   A0A1G7TES7_9SPHI        Unreviewed;      1868 AA.
AC   A0A1G7TES7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Alpha-2-macroglobulin family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05192573_103137 {ECO:0000313|EMBL:SDG33826.1};
OS   Mucilaginibacter gossypii.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=551996 {ECO:0000313|EMBL:SDG33826.1, ECO:0000313|Proteomes:UP000199705};
RN   [1] {ECO:0000313|EMBL:SDG33826.1, ECO:0000313|Proteomes:UP000199705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gh-67 {ECO:0000313|EMBL:SDG33826.1,
RC   ECO:0000313|Proteomes:UP000199705};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNCG01000003; SDG33826.1; -; Genomic_DNA.
DR   STRING; 551996.SAMN05192573_103137; -.
DR   Proteomes; UP000199705; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   InterPro; IPR011625; A2M_N_BRD.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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   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.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1003..1145
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1208..1297
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1868 AA;  208488 MW;  4B914D022DFA0874 CRC64;
     MENGYNQFRK RRTLITVVTT IALALLIIYL VAHGQKKTIV DPAFSKYIES YTTGVISKQS
     PIRIRLASDV QVTHQQNEEI NEDLFNFSPA IKGKAIWTDA RTIEFRPDEK LDPGKNYTAD
     FKLSKLIEVS DHFEHFKFNF QVIQPYFTVS FIGMQTASST SNTEMKLTGD IQTADAEDPS
     AVDKLIVPNY DSPVKINWEH DAAHKNHHFT ITGLTRIAGK ANPLTINWDG SSIGVDKKGN
     QNFEVPAIGD FKVLNIRAVQ DNDQYVEVQF SDNILVGQEL NGLISINNIT DPAYSIDGSL
     VKVYAPDRLQ GDYTISVNEG IKNTLLKRIT KGYTANLFFE NRLPAVAIPG KGVILPDSGR
     IMMPFEAINL NAVDVIIIKI YENNVPQYFQ SNGFDGSAEL RQVGKPIVQK TIRLDTDKGL
     NLHKKNRFML DLDQMIRTEP GAIYRVVIGF RRSYSLFNCK VYSGKVQKDN GDDEEGGYYG
     GDYSDNASKV SDEDDDFWKR YDNYYPEGYN WQERDDACTD SYYSKQRWAT RNIISSNIGL
     IAKRGNDNSM LIAVTDILSA EPMSNVDLEL LDYQKQVIYK TTTDGDGLAK LNLKRKPYLL
     VAKKGVQRGY LKLDDGSSLP LSRFNVGGEE VQNGLKGFIY GERGVWRPGD SIYTSFILED
     KLKTLPADHP VEFELYDPSD KLYRRITQTK SLDGFYSFHT ATETSSPTGN WTAKVKVGGA
     RFEKKIKVET IMPNRLKLSL SFGGASELTK GNNANGKLSA QWLFGGAAQN LKAKVDAYLS
     AQNTSFKKYK DYVFDDPTLA FNTQVQTVFD GKLSETGTAD VDANVNVEKQ APGQLRANFL
     VKVFEPGGNF SINQVSMPYN VYPGYVGIKT PEGSDLSGML VTDKDHLVDI ADVDVNGNAL
     PGSRDVQVEL YKVQWRWWWD QTGNEMSNFT QDKYNKLIKT EIVNLTNGAG KWKLHINKAD
     WGRYLIKIKD EQTGHSTGKI IYVDWPNWSE RLQSTNPTEA AMLSFTSDKP AYKVGDEATL
     TIPTGEAGRA LISFENGSKV LKTAWIDTKK GQTRYTFTVD ETMAPNIFVN VTLLQKHSQT
     VNDLPIRMYG AIPLQVENPE TILKPIISMP DKIRPETQSA ITVSEASGKE MTYTIAIVDE
     GLLDITNYKL PDPHDTFYAH EALGVKTWDL FDYVIGAFGG GLERILSIGG DGNLGNNKNV
     SVNRFKPVVK FLGPFHLGAG EKQTQRFILP QYVGSVKAMI VAGHNGAYGI AEKAVAVKKP
     LMILATLPRV LGPSESIQLP VTVFAMENNI KTVNIQVQSN AFSNLGGNNQ KTLTFDKPGD
     QMVTFDLNVK DFVGVGKVKI IAKSASETAA YDVDLNVRNP NPPVTRIIQK ELAPGEVWNT
     DYQPVGINGT NKAMLEVAYI PPLNLSKRLD YLIEYPHGCV EQTTSSAFPQ LYLNQLLDLS
     PKQRAETDRN IKATINRLNG FQVQGGGLSY WPYGGEADEW GTNYAGHFML AAQAKGFSMP
     IGFIDRWKKY QKEKALSWAP RKQPYYYDDD LTQAYRLYLL ALARSPEMGA MNRLREFALL
     SDAAAWRLAA AYKLAGQPEV GLRMIARLST TVKPYNSLYG TYGSDLRDEA MILETLTLLG
     QKQKAAGLVH TVAARLSQDD WYSTQTTAYS LIALAQFYGQ NKPAGKLEFN YAAGSAKATI
     STSSYLWQGA LAGNGGKVYL KNNSNNKLYI RLIQKGQPSS GQDTKSILNP DVLQMRVGYF
     SLKGKPIDPS SLKQGTDFVA QVNIKNPGKR GRYDNLALTQ IFPSGWEILN TRLLGDEAFK
     SSPSDYRDIR DDRVNTYFSL YEGQESTYYV MLNAAYTGKY YLPAVYCEAM YNNQISSLLK
     GQWVEVVK
//