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Database: UniProt
Entry: A0A142XI75_9BACT
LinkDB: A0A142XI75_9BACT
Original site: A0A142XI75_9BACT 
ID   A0A142XI75_9BACT        Unreviewed;      1915 AA.
AC   A0A142XI75;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=A-macroglobulin complement component {ECO:0000313|EMBL:AMV26723.1};
GN   ORFNames=VT84_20150 {ECO:0000313|EMBL:AMV26723.1};
OS   Gemmata sp. SH-PL17.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Gemmata.
OX   NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV26723.1, ECO:0000313|Proteomes:UP000076098};
RN   [1] {ECO:0000313|EMBL:AMV26723.1, ECO:0000313|Proteomes:UP000076098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV26723.1,
RC   ECO:0000313|Proteomes:UP000076098};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011271; AMV26723.1; -; Genomic_DNA.
DR   STRING; 1630693.VT84_20150; -.
DR   KEGG; ges:VT84_20150; -.
DR   PATRIC; fig|1630693.3.peg.4280; -.
DR   OrthoDB; 97821at2; -.
DR   Proteomes; UP000076098; Chromosome.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR   InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR   InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR   InterPro; IPR011626; Alpha-macroglobulin_TED.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412:SF136; GH01829P-RELATED; 1.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07678; TED_complement; 1.
DR   SMART; SM01360; A2M; 1.
DR   SMART; SM01419; Thiol-ester_cl; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076098};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        120..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        954..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        990..1010
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1206..1298
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   REGION          70..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          147..181
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1073..1109
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1915 AA;  208023 MW;  9E19734DFB0286D5 CRC64;
     MNPESNVIAE LQPLLDALCE EVISPDQLRR LEELVLMHPE AEEHYIRFMS FFADLIGHVA
     GLPEPKALAQ APPESVAAPA TRPAPVPRAP AEVSPAHVSP NPSPKQQENV MRRPRSLKSV
     VWLAVFGTLG ALVGSQGYGW YSRSHDVAEK QRALQIQLEE VARAEAEKAE AQRESRKHIE
     AALAAENALQ AEYQAAYESA RKAIEDKDFV VRLTGPAHIQ PGAPNKWQIE TLRHGAVGRP
     QKMDVVVKDA KDQELLRQTH DKPVGAATLE LPVAFWEKVK PGSDLFLEVT AFTDDRKSVL
     AERLPLARPV FVTHLVTDKP LYKPGETIRF RSLTLDRSTL RPPATDTHLK FRLRDPGDAV
     TTLDEGNGRL LQEIRPVLGP DNKPLRGIGV GEHTLASDAP GGEYKLDLFE ASAETGKEVL
     LETRKFIVNR YVPDTFEKKL EFDGKSYGPN EFVQARIDVS RTAGGPMKNA TANVVASTGS
     SDFFQQSNSR FTTDSTGKVF LDVRFKLSAE VFEKVAPGAA PAATLSVNIR DGSDSETIVR
     PIPLVTKTLR VEFFPEGGDM VEGVPGRVYF MVRTPNGKPA DLKGVITDGT TTFAEVSTLT
     DAENPGVNRG HGVFTLKPKA RTQYFLKLTS PNGITEPTKD GFPLPEAKAD GVALDAATEK
     GGAIRVRLQT ARGPKTVHVG AYVRERLIAQ QKVTLNAHQS TEISLKSDDT AGGVTRITVF
     EERRDDAGQA ALLPRSERLV FRGQGQHLVL NANPDRVRYT PSGKVRLDLS ATTETGAPTP
     AVLMVGVVNR SVIAMADNKN DRLLPTHFLL SGEVKNSAEL EHADFLLTDH PKAAVALDLL
     LGTQGWRRFA EQDVPPAKPV DQADVNTMLV AHGQRPTAPL QLLELEKQRV SAEFTPRLEM
     ARIQVATTEA QWSAIPAALT EKLAQAQAHV SAAQALKTEA QSALSDYKER YQRFGAALVP
     LLAAALVAIF IFIVVSSAMS ATATKPAGRL RPFIAGITTL AICGMLVLLV NNMGSNSNST
     FSFVGSSIKP PGGMVDQTVS GPVPRLGTVE GGRGTRTPRP IDDSGSMPDL DNPLRPPGAP
     AGPKASPPGP PTVGMPGAGG APPRGGKPSP KPDAGRGTSF PNHDGTFTGD VQKRLSSARS
     DKTRAALRSW SLRSPDGFAD RMPEGLIHKS DGRRSALPVI MPFMVREYAH ERDPQLGEVR
     SDFTETVYWH PVLVLPENGK STIEFQLSDD IARYQVLVAG HTLDGRIGAI TTTLEARKPF
     SVDPKLPLEI SHTDTVDAPI RVTNDSDVTR SVTFNTTATG FKTKGPLQET IELAANAKGR
     KLLRLNADQL QGDASLLIEG RSAGGDPDVI RRMIRVVPDG FPRVGSVSDM LEKGRVRGSI
     TLPKDVVPGS LRVRLEMYPT TMADLVKGLD GLLREPYGCF EQTSTTNYPN ALILDYMNQT
     NQTNPAAAAR AKGLLDKGYG RLISFECPDT PERTKHGFEW FGAADRQHEA LTAYGLLQFK
     DMARVHPVDP VLIQRTQAYL LSRRDGKGGF KRGPDGHSFG SAPKHTVDAY IVWALVESDP
     DDQEKLDLKT EIATLKAEAL NENSAGGKDA YFVALVANVM LQRGDRETAH KLLDRLKEKH
     FKNGAVTGAE TSITRSGGRD LEIEVTALAL LGWLRANDPA YGTAIKDATK WIAQQRGGYG
     GFGSTQSTIM ALKALALFAK KNAHPSESGD LGMLVGGAAV CSRQFTEQDV EVIALDVPNP
     EAIFKFGART ELEITTTAKH PYPIALSYSY TTLTPLSAEK CAVQISTKLA KNEATEGDTV
     PVAVTLENRQ KQGQGMTMAI VGIPAGMRVP TDMKQLTDLR EKGQISYFET RDRELILYWR
     ELAPEQKIAL AVDLVCDVPG TYRGPASRGY LYYDADHKHW VEPLSIKIAP MPETK
//
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