ID B8EF74_SHEB2 Unreviewed; 433 AA.
AC B8EF74;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Peptidase M23 {ECO:0000313|EMBL:ACK47192.1};
DE Flags: Precursor;
GN OrderedLocusNames=Sbal223_2702 {ECO:0000313|EMBL:ACK47192.1};
OS Shewanella baltica (strain OS223).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=407976 {ECO:0000313|EMBL:ACK47192.1, ECO:0000313|Proteomes:UP000002507};
RN [1] {ECO:0000313|Proteomes:UP000002507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS223 {ECO:0000313|Proteomes:UP000002507};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA Tiedje J.;
RT "Complete sequence of chromosome of Shewanella baltica OS223.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; CP001252; ACK47192.1; -; Genomic_DNA.
DR RefSeq; WP_006081171.1; NC_011663.1.
DR AlphaFoldDB; B8EF74; -.
DR MEROPS; M23.011; -.
DR GeneID; 11771908; -.
DR KEGG; sbp:Sbal223_2702; -.
DR HOGENOM; CLU_026846_0_0_6; -.
DR Proteomes; UP000002507; Chromosome.
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; 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; 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; 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 88..165
FT /note="Opacity-associated protein A"
FT /evidence="ECO:0000259|Pfam:PF04225"
FT DOMAIN 171..294
FT /note="Csd3-like second N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19425"
FT DOMAIN 306..400
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
SQ SEQUENCE 433 AA; 48041 MW; A0E56CA566AE45E0 CRC64;
MQTGKPNFIN LSQTRLQNLS STQKNILLMG GLLIGAAMLM PNNGHVVPTA QRIPVVLDIE
NILPQVSEPE VQDQATLINN APQFERIIVS GDTLSGLFSK AGVDQQTMYK VLEADLNILA
LDTLLPGNRM QFWLDNEGQL QKLELYFNAA RQVVFTRYED GSFNVEEVNV EGVWQNRIIS
GDIKGSFYVS AQKMGLAAAD IQRIEDLLKE KLNFARDLRV GDKFSVLVND QYVEGEATGS
SQILGVSIKT GRSEISAFQY TDGSYYDAKG QSLVRAFQRY PLAKQPRMSS RFNPYRKHPI
TGRISPHNGT DFSVPIGTKV IAPGDGVVSL VTDHQFAGKY IVIDHGGKYR TRYLHLSKAL
VRKGQRVTRG QVIALSGNTG RSTGPHLHYE FHINGKPVDP LKADIPMSSK LANQDLRTFT
NMVKSREAMM NLG
//
