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Database: UniProt
Entry: A0A4U8S5C5_9HELI
LinkDB: A0A4U8S5C5_9HELI
Original site: A0A4U8S5C5_9HELI 
ID   A0A4U8S5C5_9HELI        Unreviewed;      1796 AA.
AC   A0A4U8S5C5;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   13-SEP-2023, entry version 10.
DE   SubName: Full=Alpha-2-macroglobulin family protein {ECO:0000313|EMBL:TLD81054.1};
GN   ORFNames=LS68_006210 {ECO:0000313|EMBL:TLD81054.1};
OS   Helicobacter sp. MIT 05-5293.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1548149 {ECO:0000313|EMBL:TLD81054.1, ECO:0000313|Proteomes:UP000029872};
RN   [1] {ECO:0000313|EMBL:TLD81054.1, ECO:0000313|Proteomes:UP000029872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 05-5293 {ECO:0000313|EMBL:TLD81054.1,
RC   ECO:0000313|Proteomes:UP000029872};
RX   PubMed=25428971;
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Draft genome sequences of eight enterohepatic helicobacter species
RT   isolated from both laboratory and wild rodents.";
RL   Genome Announc. 2:e01218-e01214(2014).
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:TLD81054.1}.
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DR   EMBL; JROZ02000002; TLD81054.1; -; Genomic_DNA.
DR   STRING; 1548149.LS68_04655; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000029872; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; 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; IPR032812; SbsA_Ig.
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; PF13205; Big_5; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          923..1065
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          1132..1221
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
SQ   SEQUENCE   1796 AA;  203208 MW;  00A2B0C5F3BF8887 CRC64;
     MKHCFKIQYW LISLIVLLFV ACSDKNEIVA DYSSKIATTD EIFITFEQPI ISEENRRFIH
     QHSTKDNAIK LNGKAFEGSY SFATDSKLLI APHFPLEPNT DYTLEVNLAN LKDSHLKDKL
     KLSLHTNPTH FDYTFTHIYD KSGFNTLEAQ IEFSQKINLE NLKDSLSLKC TESKKVDFEL
     MPTSSTSIAV KSAPIAASEK EVECELTLDA KSIGLEKKEV LRYVFAGKPD LEITKIEAIP
     DANPSIEVSF SQEIKNENLQ NFVQLKPDIK AKISKSYNKL IINAPFDRLQ SYTLTLVEGL
     KAADGSKLKS NFTQDIVFTQ IPPSIAFSQQ GVFLPTNADK KISFKSMNVK KIKLKVSRIY
     PNNTTAYLYD NNLIGHKSYK DNNYYDDGIY ANFHRLGDEI INEEFDISFK PNQWIQNSFD
     LSALPNEGIF IIDLSFDENG VDYTFPDGTS NWRKRQFFDD ARIQKHLIFS NIALIAQHIG
     DKIEVLTLDI AENKPLASVD VQAISFKNQI LAESRTDNQG IAVLKTSESI MYLSATKDSN
     TTILKLNAPL SNDEFDVSGQ SIQTDTNAYI YTDRGVYRPG DSAHINIIAR ANNNPTTHPI
     YLTLISPQGK EIIEKTALTD PLYGLYYYQF DIDKNAPTGI WRVKIQVGDS VFWHNLSVET
     IIPNRIKVAI QAQDSIDMNK EDELTYGIQS HYLFGAKAAN LRYESNLQIM PVNFYPKSYT
     DYTFNHPSSL NYSFSDSQKG QLDSEGMMQD AFTLQNVENL NKNLKAFLEA KVFENGGRSV
     RAQKVIDLKL YDSFVGLKAP KTRYIDIDSN IQIPIIVLSD DEKTLIPNRN LRYRIYQNSY
     SWWWDYDNYN DFVRSIKTDR NTTLIKEGEI VSKDTPIMLD FQPKTSGETL IEVQDPSNGT
     NSAIFLYVSQ YGQPIEATKI QSFKIQSDKS NYLVGEEATI SFESKAHSKA LITLVDSQKV
     LERFWVDAKE GQTSFKVPIK KSYAPNIYVI VNLLQNYASV DNDRSQRLYG VVPLMVEDTQ
     TKLTLELKAP ESIQSNEDFT ITLSNKEHKK VAYTLAVVDE GLLDLTDFIS PNPWRYFYQK
     IALTLTSFDN FNDIIGKDIG IINQILKIGG DEAGAVAKRR KDFNEAQRFK PVVLYKSPTM
     SDEKGNATIK WKIPTYIGNV RIMAVAIDEN AYGSASRDMK VTLPVVMLPT IPRSLKLGDR
     FSLAIEVMPT ESNIGKVDIS VKSGDKITFD KKSQSLRFTS KDAQNIVFDA QVSKDSIGTE
     EIILSLTSAK FKTQEKTSID IKPNNPYTTI NKKFTIEPQG QITLSNPKDF VQNSQSGYLV
     LSQKPIMSID HRLRWLIRYP YGCIEQTTSS VLPQLYLTSL SSADFIDKPS IVKNINAGIA
     RIGNFQTSDG GFAYWQGGSQ ADIWGSNYAG HFLLLAKEEG YYVPQDLLKR WITYQINFVK
     NQTETNTAKV YSLYLLSLAK EPQIGLLNQI YENDFDSLST SDKWLLAAAY KLAGVENIVG
     KITKNLSTRV IANEHSERYY YYSYGSPLRD EAIILKAYTD IYKNSSESTQ QDRFKSLLSR
     IQTLLESDDW LSTQTLGYSL LALASTSNTR NDKADAKIQV KLDGKAFESS DIRFKIPFSA
     TNGNLESKNS TMLYANQVWD GILLDDNIQA SSSKIKLTQE FLNQNGEPIN VSTLPSGSTF
     WIKLSVDNED QSVRTNNLAV TQNIPSGWEI ENTRLNNDIL PPFVKQQGID YTDIRDDKIM
     WFFDFYGERK SVFVKINTIT PGEYILPPAT AEAMYDHSFL ANTQSSRVKV TSGVVE
//
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