ID G5NBR4_SALET Unreviewed; 439 AA.
AC G5NBR4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Cell wall endopeptidase family M23/M37 {ECO:0000313|EMBL:EHC59166.1};
GN ORFNames=LTSEINV_1968 {ECO:0000313|EMBL:EHC59166.1};
OS Salmonella enterica subsp. enterica serovar Inverness str. R8-3668.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913075 {ECO:0000313|EMBL:EHC59166.1, ECO:0000313|Proteomes:UP000003532};
RN [1] {ECO:0000313|EMBL:EHC59166.1, ECO:0000313|Proteomes:UP000003532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-3668 {ECO:0000313|EMBL:EHC59166.1,
RC ECO:0000313|Proteomes:UP000003532};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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 -!- SIMILARITY: Belongs to the peptidase M23B family.
CC {ECO:0000256|ARBA:ARBA00006646}.
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:EHC59166.1}.
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DR EMBL; AFCO01000660; EHC59166.1; -; Genomic_DNA.
DR AlphaFoldDB; G5NBR4; -.
DR PATRIC; fig|913075.3.peg.1502; -.
DR BioCyc; SENT913075:G120P-2217-MONOMER; -.
DR Proteomes; UP000003532; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
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; IPR018392; LysM_dom.
DR InterPro; IPR013731; OapA_N.
DR InterPro; IPR007340; Opacity-associatedA.
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; PF04225; OapA; 1.
DR Pfam; PF08525; OapA_N; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..141
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 439 AA; 48969 MW; 8DFD1642FD0DC6B0 CRC64;
MQQIARSVAL AFNNLPRPHR VMLGSLTVLT LAVAVWRPYV YHPESAPIVK TIELEKSEIR
SLLPEASEPI DQAAQEDEAI PQDELDDKTA GEVGVHEYVV STGDTLSSIL NQYGIDMSDI
SRLAASDKEL RNLKIGQQLS WTLTADGDLQ RLTWEVSRRE TRTYDRTANG FKMSSEMQQG
DWVNSLLKGT VGGSFVASAK EAGLTSSEIS AVIKAMQWQM DFRKLKKGDE FSVLMSREML
DGKREQSQLL GVRMRSDGKD YYAIRAADGK FYDRNGVGLA KGFLRFPTAK QFRISSNFNP
RRLNPVTGRV APHRGVDFAM PQGTPVLSVG DGEVVVAKRS GAAGYYIAIR HGRTYTTRYM
HLRKLLVKPG QKVKRGDRIA LSGNTGRSTG PHLHYEVWIN QQAVNPLTAK LPRTEGLTGS
DRREYLAQVK EVLPQLRFD
//