ID A0A0P7BV90_9BACT Unreviewed; 555 AA.
AC A0A0P7BV90;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KPM48600.1};
GN ORFNames=AFM12_08290 {ECO:0000313|EMBL:KPM48600.1};
OS Jiulongibacter sediminis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Jiulongibacter.
OX NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM48600.1, ECO:0000313|Proteomes:UP000050454};
RN [1] {ECO:0000313|EMBL:KPM48600.1, ECO:0000313|Proteomes:UP000050454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN14-9 {ECO:0000313|EMBL:KPM48600.1,
RC ECO:0000313|Proteomes:UP000050454};
RA Liu Y., Du J., Shao Z.;
RT "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL Submitted (JUL-2015) 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:KPM48600.1}.
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DR EMBL; LGTQ01000006; KPM48600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BV90; -.
DR STRING; 1605367.AFM12_08290; -.
DR PATRIC; fig|1605367.3.peg.3037; -.
DR Proteomes; UP000050454; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000050454};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..157
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 555 AA; 61916 MW; 7180E3D80B80C99C CRC64;
MNRQTALEKK KINNSKFAIR LPIIIAITLA AGIQIGAKFF GNKSVIGDVV KSSSKFKEIL
TYIDRSYVDE VDTDSLADYG IMKMLEKLDP HTAYLPAEEA ELAMSELQNG FDGIGVEFNI
YNDTVYVVTP LSGGPSEEVG IQSGDAIIEA NGTELTGEKV NTRLIFNTLR GQRGTSVDMK
IKRKGYNDLL DFTVVRDKIP TYSVDAAYLM EDKQTGFIKI TRFSETTYSE FMEGLEELKT
QGMKRLILDL RGNPGGYLER AVNIADEFIE GSGVLVYTDG KDDRNDRKIF ARHEGDFEKG
ALIVLIDEGS ASASEIVSGA LQDYDRALIV GRRSFGKGLV QAPISLSDGS ELRLTISRYY
IPSGRSIQKP YESGNLEDYY GELGHRAEHG EFFNADSVQN ENGKAYETVH GRKVYGGGGI
TPDIFVPRDT SHISRYLMEL YSNNVIREFA TSYANDHKAQ LEKMSIDAYV KNFTVDSKML
SQIRSNGEKL SIEYNAEEFR KSKEFIQQQV KALIARAIWK DRAGLSNSFY KVVNKDDEFI
KAALSHFDEA GKLGS
//
