ID A0A1I4VAA2_9GAMM Unreviewed; 1662 AA.
AC A0A1I4VAA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Alpha-2-macroglobulin {ECO:0000256|PIRNR:PIRNR038980};
GN ORFNames=SAMN05216289_101261 {ECO:0000313|EMBL:SFM98089.1};
OS Dokdonella immobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=578942 {ECO:0000313|EMBL:SFM98089.1, ECO:0000313|Proteomes:UP000198575};
RN [1] {ECO:0000313|EMBL:SFM98089.1, ECO:0000313|Proteomes:UP000198575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFM98089.1,
RC ECO:0000313|Proteomes:UP000198575};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protects the bacterial cell from host peptidases.
CC {ECO:0000256|PIRNR:PIRNR038980}.
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; FOVF01000001; SFM98089.1; -; Genomic_DNA.
DR STRING; 578942.SAMN05216289_101261; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000198575; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR CDD; cd02891; A2M_like; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.60.40.1930; -; 1.
DR InterPro; IPR026284; A2-macglob_dom_prot_bac.
DR InterPro; IPR049120; A2M_bMG2.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR040639; A2MG_MG1.
DR InterPro; IPR047565; Alpha-macroglob_thiol-ester_cl.
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; PF17970; bMG1; 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 PIRSF; PIRSF038980; A2M_bac; 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 Cell membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Membrane {ECO:0000256|PIRNR:PIRNR038980};
KW Protease inhibitor {ECO:0000256|PIRNR:PIRNR038980};
KW Reference proteome {ECO:0000313|Proteomes:UP000198575}.
FT DOMAIN 750..893
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 957..1046
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1662 AA; 181537 MW; 8D1504B0D21C7944 CRC64;
MSTLRIVSRW QSLGGAVLLL AILAIAACGK QPASVPEVQG EKPVQAEPAK AITGKFEVTS
ARAEMYQGQL ALSLEFPQQL TGAQDFDSLL SVTGANGEAV SGSWALDEDG KTLRFPFVTA
NATYTAHIKG ELSAVDGQTL GSEVSKDIFT GPLEPAVGFA AQGSVLPARE TRGLPVVSVN
VDEVDVEFLR VHDDELANFF AAYQKNARRG SWDLDPQYGW YGREGKPVAQ IADSVYANRF
VLPGNENERT LNYLPIQNIT ELAKPGLYFA VLKQPGHFRD ELETSFYFVS DIGIHTRAYK
DKMFVHAASL KTGDPISGVE IRIIDGSGNP VVTGVADESG NAMLAYTLNA AHVLVARAGR
DVSMVPFNQP ALDLSDFAVA GRRDAWFDVF AWSGRDLYRP GETVRLSALL RDNDGKSIKP
QPLFATLKQP DGRLYAEARL EPKDLGYFEW SREIPADAPT GRWQVEFRLD PASKEATQSL
TLRIEEFLPE RMKLDLATDQ AQLKPGEPLR LEVQGDYLYG APAVGNRFSA RLTLSADVHP
VEAHKDFYFG DPLIELPKEA KDVVDTALDE KGHLSEEINP LEEAKPAPVA AVLSGSLYET
GGRTVTRTLK RTVWPAEVLV GVRPLFDVKD GAGANASAGF ELIRTNAAGD LLAGDNLKLT
LVRERRDYHW IWDRESGWHF NYSERFENAE ARELKVEAGK ATRFDVPVEW GGYRIEVLDP
ATGLTLRFPF TAGWSWNDDN RGGEARPDKV KLALDKQSYR AGDTLKVTLT PPHSGPGVLI
VESDGMLYTR NIEARAGSTF EIPVTEAWER HDVYLTALVF RGGSAAERIT PARAVGEAFI
PMDRSERKVA VEIDSAKLMK PESDLAVTVK VPALAGKKAQ VTISAVDVGI LNITRFGVPD
ANDWFFAQRR LGVDAYDLYG RVIESFNGGN ARLRYGGDIG LDALPQARRP TAKVQTVDLF
AGPVDLDAEG NATVQMKVPD FNGTLRVSAL VFSEDHYGSG DTETIVRADL VAEISTPRVM
APGDKAMVSL DLQNFSGAER EFRVRVEADK PLAVGNPERK LSLADNAKST LDFPLDALEG
YGVGKIRVSA ESTDKAGDSI RVAREFEMVV RAAWPSVLRS TPQSLDSLAP VSLGSAAMDG
LLADSVNARL TLSSLPPLPF SAALADLLRY PYGCVEQTTS KGFAALLLDQ ATADKLHVEG
LDDGARKSRV EGAIGRIASM QAGSGHFSMW GGDSGVNTFI TPYVTEFLLD AREEGFVVPE
GMLQKALQRL SDDLLSGGHP YYAYDNADHL RFADEAWSAY VLARVNRAPL GTLRVLFDNE
RQKSLTALPL VHLGIALKLM GDQPRAEKAV EEAFAKTVQR PRWLGDYGSN LRDTALMVAL
VERNGMGKPE YAARVFELAR SLKTEQREAE QNQSRWGGSG RIYLSTQEQV AIGRLGKQLI
NDGDVLVSGS FAIGDTTSEF QPDRIWSRSF TAADLRAGVR LTPRGTPPLY LSTDIAGVPR
TPPEVDDSKV AIQRTFYTLD GKPWVAAPLR EGDALIVGLK LEARETMPDA ILVDLLPGGL
EIENFNLTDS KQWADVVVNG ITLSDRSNAA EVQHEEFRDD RYVAALKLNQ GQEAHVFYLV
RAVSPGTYLV PPPLVEDMYR PEIRGIGRSS VKSIKVVQPH GP
//
