ID D0MHW1_RHOM4 Unreviewed; 759 AA.
AC D0MHW1;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Rmar_1179 {ECO:0000313|EMBL:ACY48069.1};
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:ACY48069.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY48069.1, 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; ACY48069.1; -; Genomic_DNA.
DR RefSeq; WP_012843681.1; NC_013501.1.
DR AlphaFoldDB; D0MHW1; -.
DR STRING; 518766.Rmar_1179; -.
DR KEGG; rmr:Rmar_1179; -.
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 InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
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.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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..759
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023145606"
FT COILED 183..217
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 759 AA; 85474 MW; EB6B39AF7CB0BC48 CRC64;
MNQRAWIVAL SLTLAALSLR CAGPRETARI VEAPPLVTEA ETTATTGMRA AAPTALPGLD
TVRAGRFDTG RLWTFEEPPL DYWEATYGFR PDSAWLARAR LGALRLVFES GRCSGAFVSP
NGLVVTNHHC TWESLDLIDR PGEALLEEGF YADSLQGERR LPGLYAEQLL EARDVTELIV
RGLEEIRDDV ERERLRNRRL ERLKQQLEAE ARDRDTTLHV EIVPLYYGAR YTAYTWRRYH
DVRLVMTPEL RVGYFGGDFD NFTYPRYALD VSFLRVYGPD GRPLESPWYF PWSTEGVRRG
QLVFAVGNPG ATQRHLTVSQ LEFERDYTLP QRLRLLRRRA EVLERYIRQQ PDSADIYGLR
SVYFALKNTI KATEGQLRGL RDPYLLARKQ AAERALRDSM MASDSLRNYF GNVFMQLEAL
QRSKAAAAPQ TAAFQFFGTS TLLSSHILLR ALFGYAHDLM RQRGAFPSRL EELRQEALRI
RDWPDSVEVG YITARLEELR DYLGPQHPSV QRLLGDRSPA EVARDLVART ALKDSVAFAR
LLREGYLNSG DASVPVIEVL GPLYFTLGQQ LDQFEARERF LNARLAALRF AVYGHSVPPD
GTGTLRIADG RIEGYPYNGT QAPPFTTFFG MYDRFYSFRG RSGWNLPARW LTPPEAFERA
TPLNLAASTD ISGGSSGSAL IDQDLHLVGV VFDSNIEGLA GEYVYMPDRG MRAVAVDSRG
VLEALRDLYG ADRLVLELTT GKLIPDEATA EAALVGEVE
//