ID H6KZS0_SAPGL Unreviewed; 1888 AA.
AC H6KZS0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Alpha-2-macroglobulin domain protein {ECO:0000313|EMBL:AFC25846.1};
GN OrderedLocusNames=SGRA_3118 {ECO:0000313|EMBL:AFC25846.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC25846.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC25846.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC25846.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
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; CP002831; AFC25846.1; -; Genomic_DNA.
DR RefSeq; WP_015693445.1; NC_016940.1.
DR STRING; 984262.SGRA_3118; -.
DR KEGG; sgn:SGRA_3118; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000965_2_1_10; -.
DR OrthoDB; 9767116at2; -.
DR Proteomes; UP000007519; Chromosome.
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 Gene3D; 2.60.40.3710; -; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007519}.
FT DOMAIN 1016..1161
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1225..1313
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
SQ SEQUENCE 1888 AA; 211968 MW; E4587181FE404140 CRC64;
MRQLISPLFW SSLLLSGFLL FGLSACSKKN KPPTEEELFQ AADESYKNYI SAYTAGLISA
ADPIRIRFSS DLASKAQIGQ AANAELLSFE PALKGKLFWE DAATLRFEPA ENLPQKQSFR
AILDLNKLFK KLPEGLENFK FAFKALPQDF EISSHRIFIP KANQADQLEL EGALYTADVA
SPELVQQLLQ VDYPGQENLE LVWKHLADQR THQFTIKNIQ LKKGGEDGQL FLRWDGQALG
LDKKGVDTIS MPSELFKVAQ VKVLNDESGY PYFSIQFSQP LAQYTTPTTN NDIILPNNSL
QELDYISIFQ SDYEVSRRFD IFVEKNELKC IPRNKNTTGE FKLVLNEDLR SYSGDKLKGE
AEFSLELRSA QPAVRLLGRG SILPNNKGLF FPFEAINLKA VDVQVIKVYE NNVLQFLQNN
DLNDEYLNYM GRVVAQKRVS LQELAPNANP NEWTRYALAL DELIKQEPGA IYQVAIAFRK
EYQAFGCGAS ASLGLESTQA LYEEDEESQE LISFFERPEF YSYNYSRRND PCTDDYYNYS
RFVRRNLLAS DIGMIAKRGP NKEVLVALTD LRTTEPIGRA TVKIYDRFQQ LMAELQTDSD
GFAKTTTKYE PSLVVAEYNK QKGYLRMPKG GNLSLSRFEV GGSRSQTVKG LKGSLYGERG
VWRPGDSLFL TVVLESKEEP LPMQYPLKLQ LRNPRGQIVY SRTEGQHLNG VYSFKIKTED
NAPTGNWSAE VAAGGLNFSK RIMIETVKPN RLKIDLDLGK EELMAEDREL KADLKVKWLH
GAPAAKIRSR VQMSLEPMPT DFEQYPDFVF DDPTRLNYSR SPFTLFDASL NEQGFAQLQG
EIKMEALPAG KLRAGFNVRA FESGGDFSVD NFSMPFSPFT AYVGIEIPKD AGGRKTLKVK
DGNKINLVVL DQNGQPLANR KVKVGLYRLD WRWWWDNGYE NLSRFSSSYH KGAISTIELT
TDAQGKALYQ VTPEEWGRYM VRITEESSGH CTGDFFYAGS PWDDSDFGNR SAASMLAFSA
DKEVYAPGEE VVLQLPAGKT GRALLSLENG KKILEHRWIK IQDNPKGIQE IRFKVNGQMS
PTIYAHISLV QPHQNSLNDL LIRSYGVIPI RVEDPATRLE PQLEMPSKLQ PNSTVSIKVQ
EAKGRPMTYT IAMVDEGLLD LTRFKTPDLW PEFYKKEALG VKTWDLYEQV LGAFGQQLDR
IITIGGGSGM DPAQAKKANR FKPMVRYLGP FELKAGAKAE HQVKIPNYIG SVRTMLVAAQ
DAAYGQAEKT TPVRKDLMTL ASLPRVLSPK ERLALPVTVF AMEKGIKDVE VRLETNELLQ
IKGEKSKKLR FDQVGEQMLS FDIEAAEGLG VAKIKVVAQA AGKTASYELE VQVRNPNPRI
SKTYAAVLQP GENWEESLAR IGMPGTNRAS LELSRIPALN LQKRLHYLKR YPYGCVEQTV
SAVFAQLYLG SLMPLSKKES AEVEQNVKAA IKRLARFQTA TGGFAYWPGG SEASEWGSSY
AGHFLLAAKK EGYLVPQAML DNWSNYQKSM SRIWRMPRGE QLNQQSNAPL MQAYRLYTLA
LAGKSELAAM NLLRNQPLLP SNAKWRLAAA YALTGNSQLA KNMSKNLPKE VGSYREMSYT
YGSDLRDEAM ILETLNRLGQ KTEAAKVLQQ LAQKLSSDRW YSTQSTAYAL LAAADFVKQQ
KGGAQAKNSY SFSFAQLNES ASLEQAPIFE TELPVGSQSE ALKVKNTGGG PLFVQVLLEG
QALQDETEEI SNDLKLRVNY QDLEGKKLDI KQIKQGTDFI AIVEVANPGQ RGRYEELALE
QVFPAGWEIL SNRMNAALGA GNSRADYQDI RDDRVYSFFD LGAGQKMTFK IYLNAAYKGR
FYLPHQSCEA MYDHSIFANK AGGWVEVN
//