ID C3T5Z5_ECOLX Unreviewed; 686 AA.
AC C3T5Z5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Protease II {ECO:0000313|EMBL:ACI82129.1};
GN ORFNames=ECs2555 {ECO:0000313|EMBL:ACI82129.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI82129.1};
RN [1] {ECO:0000313|EMBL:ACI82129.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TB182A {ECO:0000313|EMBL:ACI82129.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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DR EMBL; EU899578; ACI82129.1; -; Genomic_DNA.
DR RefSeq; WP_000936921.1; NZ_WJRH01000002.1.
DR AlphaFoldDB; C3T5Z5; -.
DR ESTHER; ecoli-ptrb; S9N_PREPL_Peptidase_S9.
DR MEROPS; S09.010; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:ACI82129.1}.
FT DOMAIN 3..403
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 463..676
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 686 AA; 79512 MW; 0DE5B72E530948FF CRC64;
MLPKAARIPH AMTLHGDTRI DNYYWLRDDT RSQPEVLDYL QQENSYGHRV MASQQALQDR
ILKEIIDRIP QREVSAPYIK NGYRYRHIYE PGCEYAIYQR QSAFSEEWDE WEILLDANKR
AAHSEFYSMG GMAITPYNTI MALAEDFLSR RQYGIRFRNL ETGNWYPELL DNVEPSFVWA
NDSWTFYYVR KHPVTLLPYQ VWRHAIGTPA SQDKLIYEEK DDTYYVSLHK TTSKHYVVIH
LASATTSEVR LLDAEMADAE PFVFLPRRKD HEYSLDHYQH RFYLRSNRHG KNFGLYRTRM
RDEQQWEELI PPRENIMLEG FTLFTDWLVV EERQRGLTSL RQINRKTREV IGIAFDDPAY
VTWIAYNPEP ETARLRYGYS SMTTPDTLFE LDMDTGERRV LKQTEVPGFD AANYRSEHLW
IVARDGVEVP VSLVYHRNHF HKGHNPLLVY GYGSYGASID ADFSFSRLSL LDRGFVYAIV
HVRGGGELGQ QWYEDGKFLK KKNTFNDYLD ACDALLKLGY GSPSLCYAMG GSAGGMLMGV
AINQRPELFH GVIAQVPFVD VVTTMLDESI PLTTGEFEEW GNPQDPQYYE YMKSYSPYDN
VTAQAYPHLL VTTGLHDSQV QYWEPAKWVA KLRELKTDNH LLLLCTDMDS GHGGKSGRFK
SYEGVAMEYA FLVALAQGTL PARPAD
//
