ID Q9X0D8_THEMA Unreviewed; 334 AA.
AC Q9X0D8;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Endoglucanase {ECO:0000313|EMBL:AAD36125.1};
GN OrderedLocusNames=TM_1048 {ECO:0000313|EMBL:AAD36125.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD36125.1, ECO:0000313|Proteomes:UP000008183};
RN [1] {ECO:0000313|EMBL:AAD36125.1, ECO:0000313|Proteomes:UP000008183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000313|Proteomes:UP000008183};
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., Heidelberg J.,
RA Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O.,
RA Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007829|PDB:1VHO}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-334.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR001123-2};
CC -!- SIMILARITY: Belongs to the peptidase M42 family.
CC {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR EMBL; AE000512; AAD36125.1; -; Genomic_DNA.
DR PIR; B72301; B72301.
DR RefSeq; NP_228854.1; NC_000853.1.
DR RefSeq; WP_010865253.1; NZ_CP011107.1.
DR PDB; 1VHO; X-ray; 1.86 A; A=2-334.
DR PDBsum; 1VHO; -.
DR AlphaFoldDB; Q9X0D8; -.
DR SMR; Q9X0D8; -.
DR MEROPS; M42.007; -.
DR PaxDb; 243274-THEMA_09120; -.
DR DNASU; 898614; -.
DR EnsemblBacteria; AAD36125; AAD36125; TM_1048.
DR KEGG; tma:TM1048; -.
DR PATRIC; fig|243274.5.peg.1061; -.
DR InParanoid; Q9X0D8; -.
DR OrthoDB; 48055at2; -.
DR EvolutionaryTrace; Q9X0D8; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05656; M42_Frv; 1.
DR Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR32481:SF6; ENDOGLUCANASE; 1.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1VHO};
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008183}.
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 334 AA; 36633 MW; 22496B0258CF4015 CRC64;
MKMETGKLLM ELSNLDGPSG YETNVVSYIK SVIEPFVDEA KTTRHGSLIG YKKGKGIGKL
AFFAHVDEIG FVVSKVEGQF ARLEPVGGVD PKVVYASKVR IYTKNGIERG VIGMLAPHLQ
DSESRKKVLT YDEIFVDLSL CERDVRVGDI AVIDQTAFET NGKVVGKALD NRASCGVLVK
VLEFLKRYDH PWDVYVVFSV QEETGCLGAL TGAYEINPDA AIVMDVTFAS EPPFSDHIEL
GKGPVIGLGP VVDRNLVQKI IEIAKKHNVS LQEEAVGGRS GTETDFVQLV RNGVRTSLIS
IPLKYMHTPV EMVDPRDVEE LARLLSLVAV ELEV
//
