ID A3D1S5_SHEB5 Unreviewed; 468 AA.
AC A3D1S5;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Peptidase M23B {ECO:0000313|EMBL:ABN60688.1};
DE Flags: Precursor;
GN OrderedLocusNames=Sbal_1169 {ECO:0000313|EMBL:ABN60688.1};
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN60688.1, ECO:0000313|Proteomes:UP000001557};
RN [1] {ECO:0000313|EMBL:ABN60688.1, ECO:0000313|Proteomes:UP000001557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000563; ABN60688.1; -; Genomic_DNA.
DR RefSeq; WP_011846153.1; NC_009052.1.
DR AlphaFoldDB; A3D1S5; -.
DR STRING; 325240.Sbal_1169; -.
DR KEGG; sbl:Sbal_1169; -.
DR HOGENOM; CLU_026846_0_1_6; -.
DR OrthoDB; 9805070at2; -.
DR Proteomes; UP000001557; 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; IPR013731; OapA_N.
DR InterPro; IPR007340; Opacity-associatedA.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF272; BLL1407 PROTEIN; 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 SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 7..34
FT /note="Opacity-associated protein A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08525"
FT DOMAIN 113..182
FT /note="Opacity-associated protein A"
FT /evidence="ECO:0000259|Pfam:PF04225"
FT DOMAIN 205..321
FT /note="Csd3-like second N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19425"
FT DOMAIN 333..427
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 70..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 52253 MW; 83557C0AAC7BB0A7 CRC64;
MGKVITLFKL LPKKHQILLS ILSVITMITM LLPSEEAQAS RQTTSIDDQA QINTRYDVPL
AFRSPERPEL LEGQTDNAPT NATPLSSTDA LAAGDANNPA TESLESAHHR DVEHFNVKNG
DTLAAVFDRA GLTSKDVYEI TQLPLAKQNL LKIMPGEEIV ISKDINGDLT EVRYRVNAIS
TLIITKNQNQ YQEKISEKDV EIRSHFTSAK IKSNFWNAAV DAGMNANQIM QLSTVFGWDI
DFALDLREGD SFAIIYEQEY ADGEFLRNGN ILAAEFVNQD ERYTAIRYTD GNYYSENGTS
MRKAFLRSPV DFKYVSSNFN PRRLHPVTGQ VKAHRGVDYV AAIGTPIKAA GSGRVIEAGY
NQFNGNYVFI KHNDTYTTKY LHLTKRNVSK GASVKQGQII GTLGKTGRVT GAHLHYEFIV
NGVHRNPRTI TLPKAESIAR KEKNQFDTLS QQLMTTLSQN KQTQLAMQ
//
