ID   A2MG_PASMU              Reviewed;        1905 AA.
AC   Q9CMZ1;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Alpha-2-macroglobulin {ECO:0000250|UniProtKB:P76578};
DE   Flags: Precursor;
GN   OrderedLocusNames=PM0659;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Protects the bacterial cell from host peptidases.
CC       {ECO:0000250|UniProtKB:P76578}.
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}.
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DR   EMBL; AE004439; AAK02743.1; -; Genomic_DNA.
DR   RefSeq; WP_010906778.1; NC_002663.1.
DR   AlphaFoldDB; Q9CMZ1; -.
DR   SMR; Q9CMZ1; -.
DR   STRING; 747.DR93_1489; -.
DR   EnsemblBacteria; AAK02743; AAK02743; PM0659.
DR   KEGG; pmu:PM0659; -.
DR   PATRIC; fig|272843.6.peg.667; -.
DR   HOGENOM; CLU_000965_2_0_6; -.
DR   OMA; LDRYPYG; -.
DR   Proteomes; UP000000809; 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; 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   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   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; Protease inhibitor;
KW   Reference proteome; Signal; Thioester bond.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           22..1905
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000036241"
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"
FT   CROSSLNK        1438..1441
FT                   /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT                   /evidence="ECO:0000250|UniProtKB:P76578"
SQ   SEQUENCE   1905 AA;  214429 MW;  FED71CE8D61F7C78 CRC64;
     MNKQYFLSLF STLAVALTLS GCWDKKQDEA NAIQFNVNPI EITNYDETPK EVYPLVISFS
     GPAAPITSVN KELTQGISIE PALKGKWVWN SDTLLSFKPE TDWPTGQDYR VKIDKKILNP
     QLHYTQKLNE PVVFKTPEFK ATLVEQYFHQ DPTQAQVRHA IFKLSFTHPV DRQKFEKALQ
     VNLVRKNNDN TQNILSPLKF NVRYGEKDLV AWVNSDNVAL AQSDNQYIEV KIDKNLTALL
     GNNSLETDII SSVKVPTKYS LDFSTGILIA QNEKNEAEQV LHLNFTHSIK GNELEKHISA
     YLLPEFTPEN HPHWRYNLIS RDVLQHAVAV PLQRLATETT YANQQSFKLD IPEKRCLYIE
     VQNKITALGG YEMKGALGDL ACAPDYPKYV GFVGKGSILS SIGERKVTIA TRNFTKVKLE
     IGRIQEEQLR HLIALNQGNF QNPDLGQLKI DNIADFFTKN YTLNNKKPQE TTYLGIDLEK
     IVKQAEPAMG IYWLKVTGDS DNPNSTLRDT SQHMDWRNDA SNQFSDYRLI VISDLGVIAK
     KAVDGTQSVF VQSISRGEPV EGATVSVISR NGSIIKSDYT NEQGVVNFSS LAHFKQELAP
     VMYLVSTQES LSFLPIDKYD RNLDYSRFDV GGIYASENAA SLKAYLFNDR GIYRPNETLH
     TGIITKAQDW QLALNNIPLQ FNLYSPSGML MHKQTIRLEK SGLNSVSFTL PETAETGEWF
     AELLVTEKNN QTEIGSMTFQ VQEFQPDNLK IKTTFNQAHA EGWVAPQDLV ATVQLANLFG
     TPAQNRKVQA NLTLQPLLPK FSQYADYRFF DNQRNKSAIL YETELNEQVT DKEGKAHFPI
     DLTQYAENTA QMLYFTADGF ENDSGRAVST VKSVMVSAQP WLIGYQTKND LAYLKRNTPA
     VVNFIAVNPK LEKVAVEHLK ATLLERKYVS VLTQQASGAY KYESKLIENE IEQTTLQINA
     TGTDFTLNTG KSGDYVLVLS NEHDQEVNRI HYAVIGNQNV SVAMDKNTEL KLRLNKKQFK
     PHEEIEIAIH APYAGTGLIT IESDRVYAHK WFKATTNSSV QRIQLPENFE GTGYVNVQFS
     RDIHSDDIFT SPLSYGVVPF TVNVDNRRLK LQLDSPKKVK SGETVEFKLS SDKPSKALIY
     AVNEGILQVA GYQFTDPLSY FFPKYALQVQ TAQILDLILP EFSKVMQFAQ TGGDADMNME
     LAMKMAMANM NPFKRKTDKP VAYWSGIVDI HGEKTVSYQI PEEFNGNLKV MAIALSHDGK
     HLGHVATETL VRNDLILSPT VPLTLTPGDE SEINVVIANN TNKAQRVNLK ATLEPQLSFI
     GEAEKVIDIA PMSESRADFV IKATQELGSS TIRFIASYED AQQQKVDAVR HVTLSVRPIM
     PKQFATQIQK VAAGKTVTSP LPMTLFPQHR QQSALFSAAP LALAQGVSTY LTHYDNYCTE
     QMISAAMPMV LFSKNPAYQP LLTALSRKAP QNVGSTGTHD TLEKAFKLLP SRQTEYGNYG
     IWNNVEEGNL FVTAYVAHFL IEARERHLVL PKAWFGQHGL FNNTISALEE QSVPQEGDSL
     ATLRQRAYSA YLLTRLAKVP SNALLSIRTQ LEQQFSAEEW QKDTVSAWLA AAYHMLKQDN
     EANKLIEPVI NQLVAARPAQ WTYDAYSDPL IKDSTMLYVI ARHFPAQLSK VSDSVLERIV
     QDLNQQRYNT LSSSMVLLAL DAYAQQHQSE LANLQIQHQG KEISQSTPLF RFADLADTQM
     DISFVNNSQQ PAWFALSQVG YPQNAAQQAL SQGLEVDRSY TDKEGKPIRQ VKIGDVIYVT
     VKIRASTDYV SDVIITDLYP AGFEVLWQQG AEDDFEDSWL AQHTELREDR LLSYLDAEKE
     MKVLKYQLKA VNIGTFQIPP IYAESMYDRA IKAYSASEGQ IKVRK