ID F2G2J9_ALTMD Unreviewed; 441 AA.
AC F2G2J9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidase M23 {ECO:0000313|EMBL:AEA99300.1};
GN OrderedLocusNames=MADE_1015850 {ECO:0000313|EMBL:AEA99300.1};
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373 {ECO:0000313|EMBL:AEA99300.1, ECO:0000313|Proteomes:UP000001870};
RN [1] {ECO:0000313|EMBL:AEA99300.1, ECO:0000313|Proteomes:UP000001870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype
RC {ECO:0000313|Proteomes:UP000001870};
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP001103; AEA99300.1; -; Genomic_DNA.
DR RefSeq; WP_012519592.1; NC_011138.3.
DR AlphaFoldDB; F2G2J9; -.
DR KEGG; amc:MADE_1015850; -.
DR HOGENOM; CLU_026846_0_1_6; -.
DR Proteomes; UP000001870; 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:SF272; BLL1407 PROTEIN; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 81..154
FT /note="Opacity-associated protein A"
FT /evidence="ECO:0000259|Pfam:PF04225"
FT DOMAIN 178..293
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 441 AA; 49623 MW; EB53B77C738D689D CRC64;
MRKKLDASKA LHLYKNLPKQ HRTGIAIASL FLGGLILLPS EPVEASRHQE AHILDAGVRY
PVDLHITPST DVFSGEEEST WQTYKVRSGD TLAKLFKRAG FTSRDVYNVT RAGELSKTLV
TLLPGDELSF KANNDGSFGE LKYKLSSTET LFVRPDTSEE NSSLVAEVEK RAVDIRYNFA
QGEIHSSFWN AARDAGLTSN QIMNLAGIFG WDIDFAMEIR SGDTFNVVFE EQYIDGEFVG
YGDIVAAEFT NQGEHFSAIL HEDGTYYTPE GRSMRKSFLR APVNFRYVSS NFTKARFHPV
QKRWKAHRGT DYVAAVGTPI MAAGDGKVIK AGYDKYNGHH VFIQHGEKYT TKYLHFKKRA
VKVGDVVKQG QTVGYLGSSG MVTGAHLHYE FLVDGVHRNP RTVELPKALP IAKEERERFM
EIAKLRQQQL NNNKRIMLAM K
//
