TAMP_STRMB
ID TAMP_STRMB Reviewed; 760 AA.
AC P83543; N1NTU0;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Transglutaminase-activating metalloprotease;
DE Short=TAMEP;
DE Short=TGase-activating protease;
DE EC=3.4.-.-;
DE AltName: Full=Transglutaminase-activating metalloproteinase;
DE Flags: Precursor;
OS Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=35621;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29032 / CBS 199.75 / DSM 40847 / NBRC 13819 / NCIMB 11159 /
RC NRRL B-3729 / VKM Ac-928;
RA Zindel S., Froels S., Kletzin A., Pfeifer F., Fuchsbauer H.L.;
RT "Gene structures of the transglutaminase-activating metalloprotease and two
RT related putative metalloproteases from Streptomyces mobaraensis.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 230-247, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 27441 / CBS 777.72 / DSM 40587 / JCM 4778 / NBRC 13476 / VKM
RC Ac-879;
RX PubMed=12869197; DOI=10.1046/j.1432-1033.2003.03703.x;
RA Zotzel J., Keller P., Fuchsbauer H.-L.;
RT "Transglutaminase from Streptomyces mobaraensis is activated by an
RT endogenous metalloprotease.";
RL Eur. J. Biochem. 270:3214-3222(2003).
CC -!- FUNCTION: Cleaves the N-terminal propeptide of transglutaminase thus
CC activating it. {ECO:0000269|PubMed:12869197}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12869197}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; HF968452; CCW72534.1; -; Genomic_DNA.
DR AlphaFoldDB; P83543; -.
DR SMR; P83543; -.
DR MEROPS; M04.017; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SMART; SM00736; CADG; 1.
DR SUPFAM; SSF49313; SSF49313; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Signal; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..229
FT /evidence="ECO:0000269|PubMed:12869197"
FT /id="PRO_0000423083"
FT CHAIN 230..760
FT /note="Transglutaminase-activating metalloprotease"
FT /id="PRO_0000078172"
FT DOMAIN 640..760
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 32..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 454
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 760 AA; 79181 MW; D5C9591A88D3DCC7 CRC64;
MRPTPQRRAV ATGALVAVTA MLAVGVQTTS ANAGQDKAAH PAPRQSIHKP DPGAEPVKLT
PSQRAELIRD ANATKAETAK NLGLGAKEKL VVKDVVKDKN GTLHTRYERT YDGLPVLGGD
LVVDATRSGQ VKTAAKATKQ RIAVASTTPS LAASAAEKDA VKAARAKGSK AGKADKAPRK
VVWAAKGTPV LAYETVVGGV QDDGTPSQLH VITDAKTGKK LFEFQGVKQG TGNSQHSGQV
QIGTTKSGSS YQMNDTTRGG HKTYNLNHGS SGTGTLFTDS DDVWGNGTNS DPATAGVDAH
YGAQLTWDYY KNVHGRNGIR GDGVGAYSRV HYGNNYVNAF WDDSCFCMTY GDGNGIPLTS
IDVAAHEMTH GVTSATANLT YSGESGGLNE ATSDMMATAV EFWANNPADP GDYLIGEKIN
INGDGTPLRY MDKPSKDGAS KDAWYSGLGG IDVHYSSGPA NHWFYLASEG SGPKDIGGVH
YDSPTSDGLP VTGVGRDNAA KIWFKALTER MQSNTDYKGA RDATLWAAGE LFGVNSDTYN
NVANAWAAIN VGPRASSGVS VTSPGDQTSI VNQAVSLQIK ATGSTSGALT YSATGLPAGL
SINASTGLIS GTPTTTGTSN VTVTVKDSAG KTGSTSFKWT VNTTGGGSVF ENTTQVAIPD
AGAAVTSPIV VTRSGNGPSA LKVDVNITHT YRGDLTIDLV APNGKTWRLK NSDAWDSAAD
VSETYTVDAS SVSANGTWKL KVQDVYSGDS GTIDKWRLTF
