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Database: UniProt
Entry: A0A078L5K3_9GAMM
LinkDB: A0A078L5K3_9GAMM
Original site: A0A078L5K3_9GAMM 
ID   A0A078L5K3_9GAMM        Unreviewed;      1921 AA.
AC   A0A078L5K3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN59_03531 {ECO:0000313|EMBL:CDZ79213.1};
OS   Legionella massiliensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ79213.1, ECO:0000313|Proteomes:UP000044071};
RN   [1] {ECO:0000313|EMBL:CDZ79213.1, ECO:0000313|Proteomes:UP000044071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUN-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; CCSB01000004; CDZ79213.1; -; Genomic_DNA.
DR   RefSeq; WP_044012393.1; NZ_CCVW01000004.1.
DR   STRING; 1034943.BN59_03531; -.
DR   eggNOG; COG2373; Bacteria.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000044071; 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   Gene3D; 2.60.40.3710; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR011625; A2M_N_BRD.
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; IPR013783; Ig-like_fold.
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   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044071};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1058..1197
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1263..1355
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1921 AA;  211527 MW;  C768EB8E0025C23F CRC64;
     MNKSIFSQAI AKIGSIFSLV FGRIRWNSPP WAAHLHSKAK SSPLTFWTST GVLIALLAAL
     GYGYNWYKNL PKPQLIEASI TAPKITPLAE EMVPDTLSIS FGNSSEEEFV NQSVAPLNLI
     GKEVTKGIEL TPAIPGKWVW DSDSSLTFTP DEDWPAGQTY KIHFAKDAFA ATAQMASYNY
     EFSTVPFEGK ISEFKFYQDP VNPMLRQAVA TVSFNFPVDS ASLEANTNLM LQAFKFGKLD
     LKAKHYQFTI DYDEYKRTAY IHSENISLPE VSLYLILNIG KGVKSSTGSA KLAADLSQNL
     LIPDSSNYLK IGSAAASIIR NDQDRPEQIL TVESTLGVTE PEINKSLHVY LLPQNYPATA
     TEAEKTNYEW QNPGEVTSNI LALAKPLTTQ ALPSDRNYAT LHSYKFNAQS PQYIYLKIDK
     GMRGFGDFVL SNDYTAIIKV PEFPKEIGFL HKGALLALGG EKKLSVLVRG LPAVKFNFAR
     VLPENVNQLV TQTQGDFNNP YFINQSFNQQ NIAEIFSEVQ QFNASDLTQQ QYTALDFAKY
     LSATANSGGP QGLFLLQATG WDADKNEALD VNASRLVLIT DLGLVVKDNN DGSHDVFVQS
     ITQGTPVANA TLTILGKNGL GVLTRTTDAQ GRANFPSLKD FVDEREPTVY LASLGSDVSF
     MPYNKANRQL NYSRYDTGGL YSSNQELNSL SAYLFSDRGI YRPGDTAHIA MIVKQAYAKS
     QPPGLPLELT ITDPRGTTIK DQKFTLDESG FLSLDFATTD LSPTGQYIVS LYIVKDSRPY
     SLLGSTTIKV ADFQPDRMRI SSSFSQEQKQ GWISPTDLKA KVELWNLYGA PATDRTVSAK
     ILLAPKRVQF SKYPDYIFAD PLQDPNKPAK VFTDTLADSK TDDKGQAQFD LHLERFDKAT
     YQLTFFAEGF EADGGRSVAA QSTALVSPLP YFIGYKPDGD LAYIKQNGQR SVNFIAVNPQ
     LAQLKIDGLK IQLVSLHPVT TLVKASDGTY QYQSIIQSTV VDTKPFTINE QGTVYNLPAQ
     QIGDFAVNIL DSSNNELSQF KFSVVGTSQQ PLAKNAELGI KLDKEEYKAG EDIELQITAP
     YTGAGLITIE RDKVYAVQWF KADSTSSVQK IHIPDDFQGN GYVNVTFVRN WDSPEIFISP
     LSYSIAPFAV DHDNQAVHID LTTPKLALPG ETFKIGYKSD KPGKIVVFAV DEGILQVANY
     QTPDPLAFFF QKHALEVITE QTVDQILPKF IQDRELSAVG GDGGEELLAS HLNPFKRKTD
     LPVVYWSGII DTDATERELS YQIPDYFNGT LRVMAVAVAS DAVGATEKKS EIRGNFVINP
     NAPTFVAPGD EFEISVSIAN NVKGSGDNAP VTVQLTSTAG VEIIGDSTEK VEIAEGKEKT
     LHFKLRATED LGSTTLNFVA STADKSAKMD ATLSVRPATA FITSIISGST QSAKETLSPE
     RSLYPEYRKV EAALSSSPLI LVAGLQRYLE GFPYGCTEQL TSEALPLLAM SGQSWFASDT
     KAINDKIAAT VQMLGQRQMS NGGFSYWPGL GDNSSNTFAS VYAMQFLTEA RLQNYDIPAD
     LFSAGLSFLR DLAGQTPTDM DKARIQAYAI YVLTRNEIVT TNYLTNLQLY LDKDQQQKWQ
     EEITGAYIAA TYQLLQSSGE ANRLITKYKP QVKPVNATDF YDANIADAQY LYLVARHFPG
     RLPAIGDKLV MNLVKAINSS ELNTVLSGYS SLALSAYGHA NPPSSDSVFS IEEIFADSKV
     KTLTALDNSF ENVAIDEHVK QINFINPNSQ TVFYQLSQAG FDKELPTKAQ SEGVEIYREY
     RDSKGNVINS TTLGTEIEVH IQVRSLANPY LSNIAIVDLL PGGFEVVRDS VHLDNIDYAD
     VREDRVVFFT GLDTSAREIV YRIKAINTGH YTVPAIIAES MYDPNVRANS AAGGIEVRER
     S
//
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