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Database: UniProt
Entry: E1VMB7_9GAMM
LinkDB: E1VMB7_9GAMM
Original site: E1VMB7_9GAMM 
ID   E1VMB7_9GAMM            Unreviewed;      1607 AA.
AC   E1VMB7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Alpha-2-macroglobulin family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HDN1F_23760 {ECO:0000313|EMBL:CBL45959.1};
OS   gamma proteobacterium HdN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL45959.1, ECO:0000313|Proteomes:UP000002677};
RN   [1] {ECO:0000313|EMBL:CBL45959.1, ECO:0000313|Proteomes:UP000002677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA   Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with possible
RT   involvement of the electron acceptor in substrate activation.";
RL   Environ. Microbiol. 0:0-0(2010).
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; FP929140; CBL45959.1; -; Genomic_DNA.
DR   STRING; 83406.HDN1F_23760; -.
DR   MEROPS; I39.008; -.
DR   KEGG; gpb:HDN1F_23760; -.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_004561_0_0_6; -.
DR   Proteomes; UP000002677; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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; IPR041246; Bact_MG10.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412:SF136; ALPHA-2-MACROGLOBULIN HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF17973; bMG10; 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   Reference proteome {ECO:0000313|Proteomes:UP000002677};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          667..813
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          878..981
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1607 AA;  178074 MW;  6F1474E70F186425 CRC64;
     MRNHIVIDNK EFLLKDGGID LWLILITAML ISLLPAFSYA NENIPDSNYQ AQQGEAFFLL
     SDTTFSSDEI AKVRLEAPGR DHRRYSMESY GGVDIRVYRL ENPLEFLKKQ KNLHRILQEG
     SLKGEGVANA LAYLWDNWYS KSRRVMQRAF SYQTRKEVTA EVPQLKMGDA IEAPTQYQSP
     NVFAPLKGFP LVSEFRYPLW DAKPIQPPTE VKLSGSSSNF LETNPGNVYI PLGKLAPGLY
     FVEAMVGRHR ATTTVFVSNT VAISKISGNE LFVWTVHRAQ QTPVAHAKVL WTDGLGILQR
     GESDEDGTVR LLHKSPERSF VIGEDTEGGI FIAENFYYDS EVYDTRLYTF TDRPLYRPGD
     RVSFKVLGRK FSASQTSVAA GSSPVDITVI DANGTTLQTL RANYDKENGA DGEFSLPENA
     TAGGYELRVT YQGRVYSSAF RVAEYVKPHF EIAIHLDQPA FKSGEKIAGS LTLVYPDGSP
     VKNANIELRL RAQALSMVDN DLRYLGEFPV ELETKDMRSN SEGKVALSLP AADRPSRYVL
     TVFASDGAAY RVKTTREILI ERGANQYSIL GDRNFSKLNE SVTFSVHQQG IATVDAQQQI
     PSRWEWQRLE DQTRAEGSVP ENGLHFQLSF NRPGTYVIHV RDQDGKLLGA THHSVSGAGI
     VSAPGSVRIV LDKQEYQVGE TAEALVTFPE PVKDALFSLE RDHVEYAALL SRPAPWLSVE
     RIDSAQYRLL IPVTAEFSPN ITLSALYVKG SEYAFQNAGI KVPTPKLDVS VRADKSVYAP
     GDTVTVQIDT HLNGMPAPSQ LVVSVVDEMV YALQPEIAPS INDFFYRMRR NNVRTGASLS
     FISYDVATPA SGEVPSRSYR NERGVKVLER PRREEIDTAA WLPRLQTDAE GHAQFQFVMP
     DSLTRWRITV RAIRSVETAG PANATKLADG VTGQITRFIR SEKPLYLKWS GPKIFRRGDQ
     PALGVLAFNQ GSQPLKAKML ARLGDQVQER SVDLPTGVSY QAFDQINASA GDLRVSIALD
     QAPEQLLDQL DVSLSDQAAT WPEMRTLNIT LTEKETPIAL PANAFDVRMT LSNTTEQRYL
     DALSDLLDYP WGCIEQTASR LLPLSLAYPF IQSQFSGLQL NESQLNDSQF NESRNNVEIA
     GGSNELLVRL RSIMQGNRLR LVQMAGEDAT FSWWGEGTEP NALLTAYAYY ADWETSRALN
     IPLSSDHARR VLELYAKQAS DMPPLHRALA LGFLYEMRQP VSSLLSGVVK DLLQDSKSSA
     DQAADANTTQ DMAIQEVATQ AESSDTSLVF NAPDSPLGLA VTWALIAELS RRADITLPEQ
     VSSAYENAAH LLASSTLPIA RGAAIRAGWG DAKDAALLFQ EMMPSQPTFE RALLLAWFKP
     GATTTTDGAK ILPAVHPLQP WTIAPKHTTT STEWRWQGDP LPAHIVLSDV PPPTTVAVIR
     YQGEGRTESP YPVNIQRKLW LLQRGEKESH YRAEPVTAAS DGTRLQSDAL YLDEITVSTT
     ANQRLRYGLL EVSLPPGADV EPSVAGIKVA GLSDSGEVSL EKARSEPGQL SYAIPLEQLQ
     GSVRVRHLVR FSQKGQFHLP PSRYYPMYAP ARQSFEESPA MSSIVVR
//
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