ID W3TW22_BARQI Unreviewed; 441 AA.
AC W3TW22;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Carboxy-terminal-processing protease {ECO:0000313|EMBL:ETS15497.1};
GN ORFNames=Q649_00435 {ECO:0000313|EMBL:ETS15497.1};
OS Bartonella quintana JK 73.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1402976 {ECO:0000313|EMBL:ETS15497.1, ECO:0000313|Proteomes:UP000018945};
RN [1] {ECO:0000313|EMBL:ETS15497.1, ECO:0000313|Proteomes:UP000018945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JK 73 {ECO:0000313|EMBL:ETS15497.1,
RC ECO:0000313|Proteomes:UP000018945};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Kirby J., Birtles R., Dasch G., Hendrix L., Koehler J.,
RA Kosoy M., Young S., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bartonella quintana JK 73.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETS15497.1}.
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DR EMBL; AZZX01000009; ETS15497.1; -; Genomic_DNA.
DR RefSeq; WP_011178972.1; NZ_KI911825.1.
DR AlphaFoldDB; W3TW22; -.
DR MEROPS; S41.004; -.
DR PATRIC; fig|1402976.3.peg.550; -.
DR HOGENOM; CLU_017295_1_1_5; -.
DR Proteomes; UP000018945; Unassembled WGS sequence.
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 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; PF13180; PDZ_2; 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};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ETS15497.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..441
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004832627"
FT DOMAIN 84..156
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 383..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 47729 MW; FF81C571ACF51CB4 CRC64;
MIRKVILLVA GVLLGASSMI MVQSVAANNE GDTYQQLSLF GDIFERVRMQ YVTVPDDKKL
IENAINGMLT SLDPHSSYMN AEEAKDMWDS TKGEFGGLGI EVTMEKNLVK VVSPMDDTPA
SKAGILAGDL ISKIDGVQTN GQTLNEAVKR MRGAPGTPIT LTIIRSGVDK PLEIKVVRDI
IKVKAVKYRV EDDIGYLRLI RFSEQTFGDL QTAIKDIQSK IPQDKLKGYV LDLRLNPGGL
LNQAVNVSSA FLNKGEIVST RGRKKNDVVR FDAKPGDIIN GKPLIVLING GSASASEIVA
GALQDHRRAT ILGTQSFGKG SVQTVIPLGE NGALRLTTAL YYTPAGTSIQ GTGITPDIIV
EQPLPEQYKD YDVKLGESEL KGHIKGKQES NKGSGSAAFV PKDPKDDTQL SEAYKLLRGE
MAHAAFPPDP NKNVLKKDVL K
//
