ID   E1V474_HALED            Unreviewed;       443 AA.
AC   E1V474;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=CtpA family serine protease {ECO:0000313|EMBL:CBV40911.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:CBV40911.1};
GN   Name=ctpA {ECO:0000313|EMBL:CBV40911.1};
GN   OrderedLocusNames=HELO_1028 {ECO:0000313|EMBL:CBV40911.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV40911.1, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; FN869568; CBV40911.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1V474; -.
DR   STRING; 768066.HELO_1028; -.
DR   KEGG; hel:HELO_1028; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_017295_1_1_6; -.
DR   Proteomes; UP000008707; 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; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004447; Peptidase_S41A.
DR   InterPro; IPR005151; Tail-specific_protease.
DR   NCBIfam; TIGR00225; prc; 1.
DR   PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF03572; Peptidase_S41; 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|RuleBase:RU004404, ECO:0000313|EMBL:CBV40911.1};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:CBV40911.1};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU004404}.
FT   DOMAIN          105..173
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   443 AA;  47956 MW;  95856168FF0CF820 CRC64;
     MPTLCWAHSN GTARDRMPLS PTLRRRLGAI LLPIALLAAP LPVVAANETE DDLPVAEIQA
     FAEVFERIKR AYVEEVDDAT LLHNAMRGML SELDPHSSYL DAEAYENLRE STQGEFGGVG
     IEVGKRDGQI TVITPIDDTP ASRAGLQAQD TILRINDTPT EGMSLQEAVD LMRGDPGTDI
     RLTIIRQGED APRNITLERE VIRTQSVKSD TLAPGYGYLR ISQFQARTGD QVVNALNELT
     DDGPLQGLVL DLRNNPGGVL QAAVDVADAF LDDGRIVYTE GRLADSELSF YANRATTAPD
     VPLVVLINGG SASAAEIVAG ALQDQRRGVV MGTESFGKGS VQQIMPLGEN EALKLTTARY
     FTPSGRSIQA QGIKPDVEVV RGRLEVAQDN GLRVREADLE GHLSGNGKDA ESGELNARLR
     DDYQLGEALN LLKALNVLDE RKR
//