ID   D0MHW0_RHOM4            Unreviewed;       751 AA.
AC   D0MHW0;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   OrderedLocusNames=Rmar_1178 {ECO:0000313|EMBL:ACY48068.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48068.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY48068.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
CC   -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC       oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family.
CC       {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
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DR   EMBL; CP001807; ACY48068.1; -; Genomic_DNA.
DR   RefSeq; WP_012843680.1; NC_013501.1.
DR   AlphaFoldDB; D0MHW0; -.
DR   STRING; 518766.Rmar_1178; -.
DR   KEGG; rmr:Rmar_1178; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_013776_0_0_10; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000002221; Chromosome.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   PANTHER; PTHR38469; -; 1.
DR   PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR   Pfam; PF10459; Peptidase_S46; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW   Protease {ECO:0000256|RuleBase:RU366067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002221};
KW   Serine protease {ECO:0000256|RuleBase:RU366067};
KW   Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           23..751
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023013980"
FT   REGION          23..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..47
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  84570 MW;  5C45C1EAEBA0F35F CRC64;
     MKPTLRVLLS LSLALLVGCA TSQPTTTSEA PARPAPPPPP TTVPEAPLSP RMVPSLDTVR
     AGRFDNGKMW TFDDPPIDYF AEAYGFRPDS AWFREARLGA LRIPGCSASF VSPNGLVMTN
     HHCGREAVVA VSRPGENLLD NGFYARSLEE ERRAEDYYAD QLIEIRDVTD EVYAALEGAE
     TDAERAMARQ QAIQDIEQRL LEEKGGEEAG YVVEVISLYN GAKYSAYIFK RYRDMRLVMA
     PELQLGYFGG DPDNFTYPRY ALDVTFFRIY DENGEPLRTP HYFRWSREGV EEGDVVFVIG
     NPGSTSRLQT VAQLEFRRDV LEPAILRLIQ TRMAALQDYL RELPDGPERE EIRNEIFSLS
     NAEKLYTGRV KGLRDPYIIA RRRDAERRFR EALRRDSSLA RKYDPLFDRM AELVNQQRDY
     AAELQALLAF NPNSSLSSTA IRRAILAYIY LNRKQAGASD EQLAELREEI LSVDDQPKGV
     QWRYLKARLE DFVRYFGEDS RLVDQILQGR TPEAVARHII DNTVLSDSAR TAQALENGTL
     TMDDPAVQLV ATVWPRFQTF QSAWAGISAQ QQEIASQLGR ARYEVYGTSV PPDATFSLRI
     ADGVVKGYSY NGTMAPPYTT FYGLYDRYYA FGPGTDWDLP ERWLHPPETF DRSTPLNFVA
     TADIIGGNSG SPVINPNLEV VGLIFDGNIE SLPADYIYMP DRGMRAVAVD VRGILEALDE
     IYDADRLVLE LTTGQLVRSE EEADALMNSG R
//