A2MGH_NOSS1
ID A2MGH_NOSS1 Reviewed; 1906 AA.
AC Q8YM40;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Alpha-2-macroglobulin homolog {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=all5100;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. Bacterial alpha-2-macroglobulin subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved thioester bond that is characteristic of
CC the alpha-2-macroglobulins. {ECO:0000305}.
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DR EMBL; BA000019; BAB76799.1; -; Genomic_DNA.
DR PIR; AD2443; AD2443.
DR AlphaFoldDB; Q8YM40; -.
DR SMR; Q8YM40; -.
DR STRING; 103690.17134238; -.
DR DNASU; 1108704; -.
DR EnsemblBacteria; BAB76799; BAB76799; BAB76799.
DR KEGG; ana:all5100; -.
DR eggNOG; COG2373; Bacteria.
DR OMA; LDRYPYG; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041246; Bact_MG10.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF17973; bMG10; 1.
DR Pfam; PF01835; MG2; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..1906
FT /note="Alpha-2-macroglobulin homolog"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_0000036238"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 1906 AA; 211373 MW; B73C2F49C63EA92A CRC64;
MIIRVCIRCF IVLTLVLGIG GCNFFGINSG REPLPAVSPL TPPKLPDWIE QISPIGEAQP
LNQIRIRFKE ALIPVESLDS PEQQQLLQKF ALWPPLPGQF RFLTPRMVGF QADKALPIAT
RLQVTLKAGL ADLKNHRLDK DLSWTFNTQS INLTNLPGVN PIEKADAEPI DLQPKLQFTS
NVELDLASVQ EHLQLIPEGK NEGLRFQVTL NKEEKPLDKE EPLKKFDPSA RNWIYNLRPQ
KNLKTATRYR LVFSPGIRPA YGNLVTDREF VSKLSTYSPL AFQKINFYGQ PDAGGTYGRF
IKGSPQLEFN NILVAESAKT NIKINPAPKD ISRLLQVNDE DRIIGINPYA LEPAKTYTIT
IGENLQDKFG QTLGKPVSLK YDTGDLAGDI WVPSDLNIFP AGKDLRLNIS TVNLPESKYQ
AAYRVVKPTD LVYFNYGNDL LPKPAEWKSF QVSGKKNQSV DVTVPLREKI NAKTGMLAYG
VQARTNKYQE NGKELWREPT TYGLVELTNL GVFSQWFPES GLIRVNHLTD GAPVKAAVIE
IYQSKLQAKS RPEPVPCATG KTDENGTFRV NREALQQCTA GSQNSIKSPE LLVIASEKED
WAFTRTEEYS GVYGYGIDAG WQGNKPESRG VIFSDRQLYQ SGEKAWFTGF ADYLQNGVIQ
QDKNADYQIT LVNPDGQKTS LGTQTTNEFG TFSLEMPINK TQGLGYYTIQ AKGKNGLEIS
GEFRVAEFKP PNFKVEVKLD KEFAYIGDDV DINATSNYLF GAPVEGGEAK YFITRQQANF
IPKGWEEFTF GRQWFWPEEA PTISSDVLQS NSQLDGNDKS SQMVNVAKDL PYPMTYRVDV
QVADVSNLSV ANSQSFTALP SNRLIGLKSN FIADAGKAFP IEVIIADPTG KLITGQRVRL
ELQQIKYSSV TQLVEGSQTP KNQVEYKTVA QTEITSTSNP QSVNLTPPES GTYRIRVNFS
DAKNELGATD SQIWVTGGNA VFWGTRDKDV LEVKLDKKEY KAGETATALI QSPYADAELY
FAVIKDKPIY QQITKVQGSA PQIQFRVTPE MLPNAAVEAV LVRQGKPINQ VEVGSLDNLV
KIGFTPFKVN LEDKYLKLQV KPAQASLEPG AEETIQLEVK DNQGNPTKGQ LTVMVVNEAV
LQLSGYRPPN LVDTVYAEQP ISTRFTDNRP DVILQPQDVA KPKGWGYGGG FSTGAANTRT
RTDFQPLAYY NGSVLTDASG NAQITVKLPD DLTTWRVMAV ATDGNLRFGN GDATFITTKP
LLSNAILPQF VRPGDRILAG LSVTNNTGNT GNLSINGEIS GAVKFNSKNP TTTTLQTQAE
SATQAYRFPM VADSVGVGKV RFTTQLNGTA DAFELPLQVK PLEITEQIVE TGVSQKQIKI
PLNVDKNTFP EAGGLDIQLA STLIPEIKAP AKQVLTDNDL PFTEPSASQL IIATNLQTIA
QKYGQTFAEF NSRQQANLAV EKLQKLQISD GGFAAFPGQE KSDPWVSAYS VESLVKASQV
FPNLVDTGML SRLKTYLQKV LANPGEYDFC KQQLCKRQLQ LNALIALSEL GDKRNTFLTD
IYEQRNNFDL VTQIKLARYL SQFPEWQDES QQLVNKLQQN ISETGRTAVV SLPPSWGWMS
SPTTAQAQAL RLFIAKQSKP EIIDKLLQSL LALRRDGTWQ TDYNNAQALT ALVEYGQLQP
TPPNFVATVQ LAGRKLGENR FTGYKNPSLQ LSVPMNQLPR GRHDLTLQKS GNGTLHYLVA
YNYRLQGNQP GRFNGLRITR EISQVNAKRI LRKTGIYALD QPLTLALGQV FDIGLEIIVD
RPVDHLVIKD PLPAGLEAVD ASFQTTTAAL QAKADSWELG FRNIYSDRII AYADHLEPGV
YSLHYLVRSV TPGTFSWPGA EVHLQYAPEE FGRTAEMKLI VEEKGR