ID C5S1Z7_9PAST Unreviewed; 171 AA.
AC C5S1Z7;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative lipoprotein {ECO:0000313|EMBL:EER47100.1};
GN ORFNames=AM305_09481 {ECO:0000313|EMBL:EER47100.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER47100.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER47100.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER47100.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:EER47100.1}.
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DR EMBL; ACQL01000094; EER47100.1; -; Genomic_DNA.
DR RefSeq; WP_005817719.1; NZ_ACQL01000094.1.
DR AlphaFoldDB; C5S1Z7; -.
DR eggNOG; COG0791; Bacteria.
DR OrthoDB; 9807055at2; -.
DR Proteomes; UP000005532; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR47360:SF1; ENDOPEPTIDASE NLPC-RELATED; 1.
DR PANTHER; PTHR47360; MUREIN DD-ENDOPEPTIDASE MEPS/MUREIN LD-CARBOXYPEPTIDASE; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000313|EMBL:EER47100.1};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..171
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002957271"
FT DOMAIN 49..171
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 171 AA; 18842 MW; F59A0BA2511E9E01 CRC64;
MKRISKLALV SLTAILTACS SSDDVHVSGP IKAKAGIYRT NQANLGDPIM VIANLSEHQQ
EWKGTRYRLG GTSKSGVDCS GFMQITFRDL FGIDLPRTTT EQANEGRRVS KSEIKTGDLV
FFKTGRGPNG KHVGVYVKNG QFLHASTKGG VIYSDLDSPY WSKTFWQARR L
//
