ID A0A0D0GDK2_9SPHI Unreviewed; 1859 AA.
AC A0A0D0GDK2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Membrane protein {ECO:0000313|EMBL:KIO75387.1};
GN ORFNames=TH53_20655 {ECO:0000313|EMBL:KIO75387.1};
OS Pedobacter lusitanus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1503925 {ECO:0000313|EMBL:KIO75387.1, ECO:0000313|Proteomes:UP000032049};
RN [1] {ECO:0000313|EMBL:KIO75387.1, ECO:0000313|Proteomes:UP000032049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL19 {ECO:0000313|EMBL:KIO75387.1,
RC ECO:0000313|Proteomes:UP000032049};
RA Santos T., Caetano T., Covas C., Cruz A., Mendo S.;
RT "Draft genome sequence of Pedobacter sp. NL19 isolated from sludge of an
RT effluent treatment pond in an abandoned uranium mine.";
RL Submitted (JAN-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:KIO75387.1}.
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DR EMBL; JXRA01000102; KIO75387.1; -; Genomic_DNA.
DR RefSeq; WP_041885020.1; NZ_JXRA01000102.1.
DR STRING; 1503925.TH53_20655; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000032049; Unassembled WGS sequence.
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; 2.60.40.3710; -; 1.
DR InterPro; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
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; PF21142; A2M_bMG2; 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 Pfam; PF07678; TED_complement; 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 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 994..1136
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1200..1289
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1859 AA; 206191 MW; 16B9D7AFAC9CBAD1 CRC64;
MNIEQNIFIK NKKPFLIGSI AVILIGIAAF FIFRKHKSAE DQQAYAKYIE GYTSGTVSKK
SFIRIQLAGQ VKTMGEIGKP DERNLFSFSP SVKGKTFWID AQTIEFRPDE KLESGKTYTA
TFNLGKVTET EKDLEEFDFE FNVIKPGLML TQNGLISQNN TSLTYMKLTG EISTADEEDP
KLLEKCLELD FNQHLKIKWQ HNPQKNTSTF LIDSIKKTSK EEKLSLKWSG DAIDAKNKGE
ENLAVPANGV FKVLATKAVQ NLEDFALVQF SEPVGIGQDL TGLITLGTSS DLRFTIDGSQ
VKIYTPEPLL GNYMLTVNKG IVNSNERALD AAISANILFE NKLPSVTIAG SGTILPNSGK
LVLPFEAVNL KAVDVTIIKV YENNIPQFFQ NNNYKEANEL RRVGKPLLQK RIRLDEDKTL
NLHKKNRFVL DLDKIIKAEP GAMYRVTFSF RQNYNVLNCT ESSKEQTDAE YNQNGYYGEK
IDEDDDFWNS YNNYYSSEYK WADKDNPCTP SYYTSDKFAS RNLLVSNIGL VAKRGNDNSM
LIVATDLLTA KGISGVTLEL MDYQRQVIHT VKTDGDGMAS FDLKRKPFLL IAKRGEERGY
LKLDDGYSLP LSRFDVGGDV VQNGLKGLIY GERGVWRPGD SLFLSFILED KLKKLPAAYP
VTFELYNPQG QLIKKAVSGA SLNGFYAFRT STESTAPTGN WSVKVKAGGA SFQKSIKIET
VMPNRLKIGF DIGSRKYLGT GAAAPATLSA NWLFGATGKN LKAKVDVNLN TMKTTFPGFD
GYNFDNPTVN FVSQVKTIFE GRLNENGMAA VNTNLNDNAT APGVLKANFT TKVFEAGGNF
SIDNFSIPYH VFTNYYGIKA PEGEKLSGML MTGKDHNFSI VNVDRNGKLL SGSKTVQVEL
YKVQWRWWWE QDTQNSFANF TQNEYNKLIR KGNVVLQNGK GNWTLHIDEP EWGRYLVLVR
DAEGGHVTGK AVYVDWPGWA QREQSANPTE ASMLSFTANK TKFKVGEDIV LTIPTGENGR
ALISLENGSR VLKTFWTDTK KGQTQFKFKA EKNMAPNIFA NITLLQPHAQ TVNDLPIRMY
GVIPLVIEDP ETILKPVIKM ADKIKPETEN TITVSEQNGK AMTYTIALVD EGLLDLTRFK
TPDAHAVFYA REGLGVKTWD LFNYVLGAWG GNLERILSIG GDGSVNRNLN PAKANRFTAV
VKYMGPFALG KGGSQTHKFK LPQYIGAVRA MVVAGQDGAY GSAEKSVQVK KPLMVLATLP
RVVGPGESFT LPVTVFATEN NLKNVAVQLQ TQNLQVSGLK TRQLTYAQPG EQMAYFDVTV
PQITGIAKVK IVAQSGAEKA VYDLELDIRN PNPYVTNVVS AIIQPGQSWT TDYLPLGIAG
SNSGSVELSS IPPVNLKKRL SYLMQYPHGC VEQTTSSVFP QLFLNKLSPL NEQQKAQTDR
NIKAGINRLR SFQTTEGGLA YWPGDPSADE WGTNYAGHFL VEAQNSGYNI PVGMLDEVLR
YLKGKAGSWV PNSNNFYGGD LSQAYRLYVL ALARKPEMAA MNRLKAFEYL SVSAKWRLAA
AYQLAGQASA ATALTKGLDI TVKPYTQLGG TYGSDSRDEA MILETLTLMG QKGRAAQVLQ
TVAAKLGTDD WYSTQTTAYG LLSIAKFCGQ NSASSRLNYT YLLDGKKGTF NQNQYLSSLP
INFKGKTAAV TNNGQTVLFA RLILDGQPAA GQNNFKPNNS DILDMSVSYK LLNGKPIDPS
VLKQGLDFYA EVVLKNPGKM GLYEQMALTQ IFPSGWEIIN TRVNDNESII ASSPYTYRDI
RDDRVFTYFN LRENETVTYK VLLNASYIGK YYLSAIQCEA MYNNTISATQ NGKWVQVIK
//
