ID F4C9I5_SPHS2 Unreviewed; 1834 AA.
AC F4C9I5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Alpha-2-macroglobulin domain protein {ECO:0000313|EMBL:ADZ80657.1};
GN OrderedLocusNames=Sph21_4125 {ECO:0000313|EMBL:ADZ80657.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ80657.1};
RN [1] {ECO:0000313|EMBL:ADZ80657.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ80657.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) 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; CP002584; ADZ80657.1; -; Genomic_DNA.
DR STRING; 743722.Sph21_4125; -.
DR KEGG; shg:Sph21_4125; -.
DR PATRIC; fig|743722.3.peg.4397; -.
DR eggNOG; COG2373; Bacteria.
DR HOGENOM; CLU_000965_2_1_10; -.
DR OrthoDB; 9767116at2; -.
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; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR011625; A2M_N_BRD.
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; IPR013783; Ig-like_fold.
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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1834
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003306386"
FT DOMAIN 972..1114
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 1177..1268
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT REGION 444..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1834 AA; 205902 MW; 4B23DCC193E1CB64 CRC64;
MKKKYLFIYF LFLLVACAKK NGKDFNSDFS LYKDYITEFT SGIISAKSTI RIVLNFNTKE
WMPNQELESN LFEITPKVEG KVIALSQNTL MFKPSKRLKQ DTEYQISFKL KELIDVPKEL
KEFNFTIKTI KQDFVVLSRE LQSYSSEYQF QHAILRTSDE MDAQSAAKLI YAKQGTGKLP
IRFDQIKSGT EFRFIVDSIK RPEKDGSIQL MWDGSDLDID QKGEEEIEIA AKGHFKVMKA
TVAEENNQLL LINFSDPLKK SQDFEGLVTI DSAKSLTYTV DGNVLKVFLS EPLKGERLLE
VFQGVESAQG TKLKKGYTKK VYFEQTKPGV RLLKNGTLLP SSNNLKLNFE AANLKAVDVK
IYKIYQDNIL QFLQDNDLNG SYNLRKVALP IAKKKIELTQ NRLYNNGKWN VFALDLASLI
KPDPGAIYHV EFSYKKAYSI YPCSSQPEEN QEEPEEQSLE DEQASFRSNE SEDYPYYDDY
NWQEREDPCA NSYYYYDNKV STNVLATDLG VIAKMGKNGS YFFAVNNIVT TEVVPGAHIE
LYDYQQQKVG EATTNDEGIA HLDHTKRGYF VIVKKDNSST YVKLEEGLSL SLSNFDVAGN
ELEKGLKGYI YGERGVWRPG DTLFLSFMLN DQANRLPANH PIKLRLTDPN GKLFTQLVQR
SNERNLYRFV IATKDEAPTG NWEAVVSVGG ARFYKSIKIE TIKPNRLKIK NNLAGRVLQA
NSATTDEISV IWLHGAVAKN LKAEMQAKFY QMKTTFKGLA NYVFDDPARS FSTEEVNVFS
GNVDENGKAT IGIKPQLHGQ APGMLKASFI TKVYENGGDF STDVATATYS PYQTYVGLKS
PEPNKYGMLE TGKSNRFDIV TVDEKGRPKA VANLEVKIYK VDWRWWWDAS NDNLSSYSAS
SSKTPFKSYR ISTGTSGKTS VQFVVNDEDW GRYFVRVTDL DGGHASGETV LIDWPYWSAK
TKNTDGTNAN MLVFSTDKPK YNVGEKMKIS FPSSERSRAL VSIESGAKIV NTYWVETKKG
ETQLEVPVTS EMAPNIYLFV TLLQPHASTL NDAPIRLYGV VPVEVLDKET ILQPVLSMLD
VLRPEQAVNL QVKEKNGRAM SYTIAIVDEG LLDLTRFKTP NAWDKFYARE ALGVKTWDVY
NDVIGAYGGK INQVFSIGGD EDIGGGENKH ADRFKPVVIY LGPFHLSKNE SKTHRVKLPN
YIGSVRTMVV AGDAKTSAYG STEKATPVRS PLMVLASLPR KISPGEKVTL PVTVFAMENQ
IKNARVQVKV SKGIKVLGSS AKSLSFSGPD EKMVYFDLEV GTLTGMAKVE VVASSGNERA
SYPVEVDVTN PNPVTHDYKE LVLKANEEQT LTWEPFGVDG SNKARIELSS FPSIDLNARL
NYLIQYPHGC LEQTTSSVFP QLYLGDIVDL EAAKREAIQR NVVEGISKLA GFQLPDGGFV
YWPGLSSADD WSTSYAGHFL LEAETKGYVL PIDFKNKWIS YQQRAARQWR METHPGSDFA
QAYRLYTLAL AGAPDLASMN RLRETVGISN EARLRLAAAY VLAGQKHAGN ELLKISSINN
VNNAYSYYYY GSPERNRAMV LETLLLLNRT VDAFALATKI AKDLSSGAWM STQTTAYSLY
SIAKFAKLNG KNGVNARFSY HGQSADVKTT KSFIDKGLQI NKGLNSIKIR NNDKNTLYVK
LLNSGVLPVG REQVIQRNLT VQVEFVDRAG GTLDIHTLKQ GTEFVALVAV KNQSLDRVEN
LALTQILPSG WEIVNTRYTD YGAFGQNKAD YIDIRDDRSS FYFSLNGNES RTFKILLNAS
YLGRYYLPGV QCEGMYDHSF LTRTKGTWVE VVDY
//
