ID F7XVF2_MIDMI Unreviewed; 679 AA.
AC F7XVF2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Protease II {ECO:0000313|EMBL:AEI88651.1};
GN Name=ptrB {ECO:0000313|EMBL:AEI88651.1};
GN OrderedLocusNames=midi_00341 {ECO:0000313|EMBL:AEI88651.1};
OS Midichloria mitochondrii (strain IricVA).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Candidatus Midichloriaceae; Midichloria.
OX NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88651.1, ECO:0000313|Proteomes:UP000006639};
RN [1] {ECO:0000313|EMBL:AEI88651.1, ECO:0000313|Proteomes:UP000006639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IricVA {ECO:0000313|EMBL:AEI88651.1,
RC ECO:0000313|Proteomes:UP000006639};
RX PubMed=21690562; DOI=10.1093/molbev/msr159;
RA Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT the free-living mitochondrial ancestor.";
RL Mol. Biol. Evol. 28:3285-3296(2011).
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DR EMBL; CP002130; AEI88651.1; -; Genomic_DNA.
DR RefSeq; WP_013950866.1; NC_015722.1.
DR AlphaFoldDB; F7XVF2; -.
DR STRING; 696127.midi_00341; -.
DR MEROPS; S09.010; -.
DR KEGG; mmn:midi_00341; -.
DR HOGENOM; CLU_011290_0_1_5; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000006639; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AEI88651.1};
KW Protease {ECO:0000313|EMBL:AEI88651.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006639}.
FT DOMAIN 17..396
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 457..668
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 679 AA; 79101 MW; 9828D80C8E4264F4 CRC64;
MTKPIALRKE YKTIDGRIDY YHWLRDPNWP DVKDPEILSY LNQENAYTDA HISKDLVDKI
FIEMRGKLEE ADKTVPYLNG WYYYYSYILE GQQYWIHARK KENNEREEIL LDENQLALNE
KYLRVSTLKI SPDHKKIAYL ADYGGDERYM VYVKDIESGE IIENNVDDVI GNIEWDGLGK
GFFYTPAGKF WRADRIYYHE VGKEKKDDKL LYQEKDNTFS VAIEKSSSKN YIFFMSKSAT
ASEYHFIDSR NPHQLPQVIH SRTNNHIYEV VHTRDSFFLR INDVAPNFRV IQVSINDLKN
WQEFVPSSDY YIQDIYAYED YLVLLTRLKG RAKIEIINLL ENKIQRIDVE GEFYEIFIIH
NTFNDRALRY LYSSLKTPRT TIDYDFVTGE KKVLKVQRIP GGFDPSKYIL RRIWAETSDN
ISIPISIIYN KEKAKLDGSD PLYLYGYGSY GYAVPASFRS HIFSLVDRGF TYAIAHIRGG
DELGKSWHEA AKFLNKKNTF TDFIESAEKL IEDKYTAPGK IVISGGSAGG MLVGACINMR
PELYKAAVAH VPFVDVLSTM LDESLPLTPG EFKEWGNPKE KEFYEYIKSY SPYDNVVPQR
YPHLFVTAGL TDPRVTYWEP AKWVALLRHT KKDDNMLLLK TDMSSGHGGP SGRFEFLREL
ALEYAFILGL YYGEQHINN
//
