ID   CTPA_BARBK              Reviewed;         434 AA.
AC   Q44879; A1URP1; P70869;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Carboxy-terminal-processing protease;
DE            Short=C-terminal-processing protease;
DE            EC=3.4.21.102;
DE   Flags: Precursor;
GN   Name=ctpA; OrderedLocusNames=BARBAKC583_0324;
OS   Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=360095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9141685; DOI=10.1099/00221287-143-4-1221;
RA   Mitchell S.J., Minnick M.F.;
RT   "A carboxy-terminal processing protease gene is located immediately
RT   upstream of the invasion-associated locus from Bartonella bacilliformis.";
RL   Microbiology 143:1221-1233(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35685 / NCTC 12138 / KC583;
RA   Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA   Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA   Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA   Fraser-Ligget C., Seshadri R.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RA   Minnick M.F., Mitchell S.J.;
RT   "An alpha-helical coil protein encoded upstream of the invasion locus of
RT   Bartonella bacilliformis.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in protection of the bacterium from thermal and
CC       osmotic stresses. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=The enzyme shows specific recognition of a C-terminal
CC         tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa
CC         is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves
CC         at a variable distance from the C-terminus. A typical cleavage is
CC         -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.;
CC         EC=3.4.21.102;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: May undergo autocatalytic processing at the C-terminus (398-434 or
CC       425-434 missing).
CC   -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
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DR   EMBL; L37094; AAB61766.1; -; Genomic_DNA.
DR   EMBL; CP000524; ABM45226.1; -; Genomic_DNA.
DR   EMBL; U73652; AAB18238.1; -; Genomic_DNA.
DR   RefSeq; WP_005766244.1; NC_008783.1.
DR   AlphaFoldDB; Q44879; -.
DR   SMR; Q44879; -.
DR   STRING; 360095.BARBAKC583_0324; -.
DR   MEROPS; S41.004; -.
DR   EnsemblBacteria; ABM45226; ABM45226; BARBAKC583_0324.
DR   KEGG; bbk:BARBAKC583_0324; -.
DR   PATRIC; fig|360095.6.peg.308; -.
DR   eggNOG; COG0793; Bacteria.
DR   HOGENOM; CLU_017295_3_1_5; -.
DR   OMA; TFNQVDW; -.
DR   OrthoDB; 1646508at2; -.
DR   Proteomes; UP000000643; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07560; Peptidase_S41_CPP; 1.
DR   Gene3D; 2.30.42.10; -; 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   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00225; prc; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..434
FT                   /note="Carboxy-terminal-processing protease"
FT                   /id="PRO_0000027334"
FT   DOMAIN          86..166
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          383..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        294
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        305
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        319
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   434 AA;  47269 MW;  11B9924F27FE63A4 CRC64;
     MIRKVIFFVA GVFLSASLIV MAQSITTNNE QNTYKQLARF GDIFERVRTQ YVTIPDDQKL
     IENAINGMLL SLDPHSSYMD AEKAKDMRDS TKGEFGGLGI EVTMENNLIK VVSPIDDTPA
     AKAGVLAGDF ISKIDGKQIS GQTLNEAVDQ MRGPAGTPIT LTINRFGVDK PLDIKIVRDI
     IKVKAVKYRV EGDIGYLRLI QFTEKTFSDL QAAIKDIQSK IPTDKLKGYV LDLRLNPGGL
     LDQAISVTDA FLNKGEIVST RGRKQNDVMR FDAKLGDLTD EKPIIVLING GSASASEIVA
     GALQDHRRAT IIGTQSFGKG SVQTIIPLGE NGALRLTTAL YYTPSGTSIQ GIGITPDIVV
     EQPLPEKYKG YDVTLGESEL RGHIKGKQES DKGSGSAAFV PRDPKDDVQL NEAYKLLRGE
     ITHAAFPPDP NKVF