ID I3DE40_HAEPH Unreviewed; 462 AA.
AC I3DE40;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Peptidase, M23 family {ECO:0000313|EMBL:EIJ69983.1};
GN ORFNames=HMPREF1050_0715 {ECO:0000313|EMBL:EIJ69983.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ69983.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ69983.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ69983.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:EIJ69983.1}.
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DR EMBL; AJSW01000037; EIJ69983.1; -; Genomic_DNA.
DR RefSeq; WP_005706702.1; NZ_UGHI01000002.1.
DR AlphaFoldDB; I3DE40; -.
DR MEROPS; M23.011; -.
DR GeneID; 78223814; -.
DR PATRIC; fig|1095744.4.peg.1231; -.
DR OrthoDB; 9805070at2; -.
DR Proteomes; UP000003016; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 3.10.450.350; -; 2.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR045834; Csd3_N2.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF291; MUREIN DD-ENDOPEPTIDASE MEPM; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF19425; Csd3_N2; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 201..323
FT /note="Csd3-like second N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19425"
FT DOMAIN 335..429
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 34..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 51766 MW; 09A74D3C78E4BAD4 CRC64;
MAVLSIGIGI ALSLKKQTPR NESSQENVII LDNLDNDIID DVENPNSDTE QAEKKQDLTE
DPNATSYDDE LASEDDEEEG EEGKSKVLQE KLPEEAEQLI SDIVNIADEA LRIQDQFSYV
VTKDDKLSDV LEQSGLGDDD ARALIFQYPE LGKLEVGQQF YWVLDNFGEL EYLNWLVSEK
EERIYERQEH GKFSYQRIEK KGVWRQDVVK GEIQGSFTTS LRNVGLSDRQ IKQLAVGLQS
QIATSKLKNG DSFAILVRRE YINDTVTDIG NVEGILIESS NKRYYAIQAS DGRYYSNHGE
TLTKGFARQP LLFTARVSSP FNPRRLHPIT KRVRPHNGVD FGIPMGTPII APSDGVVEHV
AFQAKGAGRY IKIRHGHITT VYMHLSKPLV KKGQTVRKGE RIALSGNSGG STGPHLHYEF
HINGRPVNPM TVKLPGSGSG MASKDRKNFL ERVKNVQAKL KL
//
