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Database: UniProt
Entry: M5DTN6_9GAMM
LinkDB: M5DTN6_9GAMM
Original site: M5DTN6_9GAMM 
ID   M5DTN6_9GAMM            Unreviewed;       712 AA.
AC   M5DTN6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Periplasmic tail-specific protease {ECO:0000313|EMBL:CCU72557.1};
GN   ORFNames=TOL_2152 {ECO:0000313|EMBL:CCU72557.1};
OS   Thalassolituus oleivorans MIL-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Thalassolituus.
OX   NCBI_TaxID=1298593 {ECO:0000313|EMBL:CCU72557.1, ECO:0000313|Proteomes:UP000011866};
RN   [1] {ECO:0000313|EMBL:CCU72557.1, ECO:0000313|Proteomes:UP000011866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIL-1 {ECO:0000313|EMBL:CCU72557.1,
RC   ECO:0000313|Proteomes:UP000011866};
RX   PubMed=23599290; DOI=10.1128/genomeA.00141-13;
RA   Golyshin P.N., Werner J., Chernikova T.N., Tran H., Ferrer M.,
RA   Yakimov M.M., Teeling H., Golyshina O.V.;
RT   "Genome Sequence of Thalassolituus oleivorans MIL-1 (DSM 14913T).";
RL   Genome Announc. 1:1-3(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; HF680312; CCU72557.1; -; Genomic_DNA.
DR   RefSeq; WP_015487277.1; NC_020888.1.
DR   AlphaFoldDB; M5DTN6; -.
DR   STRING; 187493.CN03_07480; -.
DR   MEROPS; S41.001; -.
DR   KEGG; tol:TOL_2152; -.
DR   PATRIC; fig|1298593.3.peg.2051; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_016199_1_0_6; -.
DR   Proteomes; UP000011866; Chromosome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00988; PDZ_CTP_protease; 1.
DR   CDD; cd07560; Peptidase_S41_CPP; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 3.30.750.44; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   InterPro; IPR020992; Tail_Prtase_C.
DR   InterPro; IPR040573; TSP_N.
DR   NCBIfam; TIGR00225; prc; 1.
DR   PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 3, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR   Pfam; PF11818; DUF3340; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   Pfam; PF17804; TSP_NTD; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004404};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011866};
KW   Serine protease {ECO:0000256|RuleBase:RU004404};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..712
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005689140"
FT   DOMAIN          246..321
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          620..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  79971 MW;  F0E929EC6A32BE66 CRC64;
     MFSQKQYILR PLCTGLLAMF SMASVATIPD IAPGTPFTPL QPAQEHAVTT QQIMSNLLRG
     HYERKRLDNA MSSQVLDTLL DDIDSTRSYM LASDIAEFEQ YRTSLDEALS RGNMAPAFSI
     YNRFEQRVAE RLSFLLNELS NHVKDYNYKQ DETLELDRED APWATTAAEL DELWRKRLKN
     SILNLKLAGK EQDDIIKLLT RRYQNQLNRV YLSKPEDAYQ TFMNAVTRTF DPHTQYFSPR
     NSENFNINMS LSLQGIGAVL QTEDEHTKVV RLVPGGPAAK ANNLSPADKI VGVGQDADGE
     IVDVIGWRLD EVVDLIRGAS GTTVRLEILP ADSSGSDSKV ISIVRDEVKL EEQSAQKEII
     ELKDGDKTRR IGVIDIPTFY IDFQGRMENR PDYKSTTRDV RKLITELKEE GIDGLIIDLR
     NNGGGSLEEA IDLTGLFIPT GPVVQVRGIR DRVEVLQDQD PEVLYDGPMT VLVNRLSASA
     SEIFAGAIQD YGRGLIVGGQ TFGKGTVQSL RPLTQGQLKI TQAKFYRVSG DSTQHQGVIP
     DVLFPSLFDK EKIGESALKA ALPWDTIQPA RKAGINTITP TLPHLRELHD ARIEHNPDFL
     FLREQKEMIT EMRDKTEVSL NEEVRKKERE ANDERRLSLE NKRRKAKGME LLTALDDAAS
     NGEETPAKAE ADKSDETKKP EEEDAILEEA GYILLDYEHM TQGAMTAQRL DN
//
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