ID   A0A1W6MN42_9FLAO        Unreviewed;      2177 AA.
AC   A0A1W6MN42;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alpha-2-macroglobulin domain-containing protein {ECO:0000259|SMART:SM01360};
GN   ORFNames=BST97_14120 {ECO:0000313|EMBL:ARN79033.1};
OS   Nonlabens spongiae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=331648 {ECO:0000313|EMBL:ARN79033.1, ECO:0000313|Proteomes:UP000193431};
RN   [1] {ECO:0000313|EMBL:ARN79033.1, ECO:0000313|Proteomes:UP000193431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13191 {ECO:0000313|EMBL:ARN79033.1,
RC   ECO:0000313|Proteomes:UP000193431};
RA   Kumagai Y.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; CP019344; ARN79033.1; -; Genomic_DNA.
DR   STRING; 331648.BST97_14120; -.
DR   OrthoDB; 9767116at2; -.
DR   Proteomes; UP000193431; Chromosome.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.50.10.20; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.170.130.10; TonB-dependent receptor, plug domain; 1.
DR   InterPro; IPR041246; Bact_MG10.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR001599; Macroglobln_a2.
DR   InterPro; IPR002890; MG2.
DR   InterPro; IPR012910; Plug_dom.
DR   InterPro; IPR037066; Plug_dom_sf.
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; PF17973; bMG10; 1.
DR   Pfam; PF13715; CarbopepD_reg_2; 1.
DR   Pfam; PF01835; MG2; 1.
DR   Pfam; PF07715; Plug; 1.
DR   SMART; SM01360; A2M; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF56935; Porins; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193431};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..2177
FT                   /note="Alpha-2-macroglobulin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012845762"
FT   DOMAIN          1416..1506
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   COILED          31..58
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2177 AA;  250257 MW;  0B8098407C1D7ED2 CRC64;
     MKFYYLLLIS LTCSLAMAQK PFDKKWEEVE LLEVQNKIDD AQKIVKRIKR KAQRRDNESQ
     LIKAFIYKAK FDLINSSGAL SDVESELQQL IRTSNSPSRN IYQMIYAELL ENFKDRESSN
     LREREKFDIK IDSTDHRAWD LSYLNQKIKQ LYDSSIENPE ELSKISIDEY AAIITDTLYT
     KKWQPTLYDL LARSAIENLK DEINPYFMST EVDSIYLQEA VKLKPDLTKI KPSNSFETKF
     KQIIEIYQQL ENIHLFTHRE AAYIKVVIDR INFVPTNNDD KLIKTYEESL SALSTEYSHE
     PEHTLATYQL AKHFFSKANV DQYLRRDSKK ESNRLRVKYR AKAIELALQS IEQFPKSFGA
     RQCKSLLEVS RSSSINIRFE PISYPEQYSI AQIDHKNIDS LKVFWKRISI TDYINLEDSL
     ADAIYNSAKT ENSFERIVEI DLKTEHDGFR EQLNYPWQAP KSEGNYLIYL EYKTGNITKI
     DYEQAQVTSI LPQATYDDDR AYFKVLERFT GYPLKGVRVQ MQEDEELPVV EVVTDFDGMA
     IANIKDFDDS HSLLFIRGKD SLLLDNYSLY SNYEDKEEEV DEKTVTTYVY LDRGIYRPGQ
     TVYYKVIVVV EENGSTRVLP NEELNFYVES ANGREIFDIY QTTNEYGSFH GSFEIPEGVA
     LGEFSIDIDS DEETIFWDIV DGINGWDTAK TFRVEEYKRP TFEVTIEEKD RKFLVGSNIQ
     LKVNAKAFLG APIDGAQVNY SIYRKSYDYG NLRYSYGYDK IDSKTFKNDS ITTNTKGEYI
     IDFIAEPNNY KEKENDQKLN YAYKIEVEVL DANGEQHDAQ TVVEASSKAH ELILETPAEI
     SLNNRSISFY SENLTKQKIE KSYQIKIYKT TGEYRNTNDP WSETGLSRKK LDSLFADDLN
     YKFNFAKQKD SLVFSKVYEH QETVQTELPI DSSWKNGFYR IEVETLSVDA EKSPLKTSKT
     LPFWINKNQP LTPLLAMENH RFTDEGVDID FFTSADSTYV SMYVFTHDKD LREESFTIYK
     GKTTHSTTYS EVPGSITYFK YETTRKGATG SGMLSIERTR EEQGAIRIKT ETLRNKLQPG
     KEETWSFQLE NENGSPFQLE ALASMYDASL DDFKENEWMP LKPLDTYRYN KREPFKYYMT
     LRNYYGYAYY SGGTSYGYGL LSLPSGPHWV FHGLLQADYH SLYRSYLESL KLKRKDKKKL
     KKGAHLLGVV TGPDGLPILG ATVQILDTQT FTTTDFDGNF SISAETGDTI LISYTGYDSQ
     QIIVGKSNYK EIQLTTSLDE VVVTGYRTIL GVPPPNSNAI QRLMGQVPGV TVQTATGQPG
     ANSLNQIRGV SSMNENTEPL IVFDGKPITE KQFGLLSRET IGEVTVIKPE DATAIYGNRG
     SNGVIIITPK KGFNYEELLN LESLANVETR KNLDETAFFL PQLYTDQKGS LKFTFTSPEM
     LTRWNFQLLA HNKNAESSII SREVVTQKDL NIILNKPRFV REGDYLVLKA KLINLTNKDI
     KALCKLEFSN ASNMKKLNII EGPSLKNLSI GNKSSQNLSW KIKVPENLPA LSYKIIASAG
     NFSDGEEGVI PVLPNKILVS RTTRSWIASK GTGEITLPDL TRENINKYDS KNLSFEFQGS
     PKIAIIYALP YLMDYAHQCS EQTFAKYYAN AVAAHLVQSD PEIAQFIKQN HQNSNPEEEP
     LQSAINSSPW YYKLASPQVK LERLVSYLEP EKVQDQQSRH LQRLKLMQDS DGLFPWFDGG
     APNISITQHI LNGLSFLKHK NLLTQDEFPS FMYEKGLQGL DSYWKEYLED FDKQYNKGVE
     SFTFSTTYWD YLYVRSQEKD VEVKTDSTDI LGRVKDLAFA KAKKQFATYS IYEQLLMAMT
     LHNEGHNKEA KNILQGLRQI AVKNDERGMY WKFHENNRGW YGRAIETQSL AITAFSQILN
     DTNTVELLKI WLLNKQEWAS WGTTKATVMA STAVLETSGK ATEIQMPKIY WGGTSITEQQ
     NISQGSMEAL NSITGNVPIE DIQESYKTLK IDNKSDQPAT AAIHWDFMAP LEEFNALEDD
     DVKVNKKLYH KDDSNQWLEL THGDILELGE KIKVKLLIET TKNLSYIHLK DLRASGLEPV
     ETLSEHSRVN GTTYYKSIRD DRHDFYFELM QAGTYVIEYE LMCNNAGVFE NGFARMEGMY
     NPELKVYSKS MRIKIQD
//