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Database: UniProt
Entry: H0IY91_9GAMM
LinkDB: H0IY91_9GAMM
Original site: H0IY91_9GAMM 
ID   H0IY91_9GAMM            Unreviewed;       551 AA.
AC   H0IY91;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Peptidase M23B {ECO:0000313|EMBL:EHK62382.1};
GN   ORFNames=MOY_01649 {ECO:0000313|EMBL:EHK62382.1};
OS   Halomonas sp. GFAJ-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK62382.1, ECO:0000313|Proteomes:UP000004512};
RN   [1] {ECO:0000313|EMBL:EHK62382.1, ECO:0000313|Proteomes:UP000004512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62382.1,
RC   ECO:0000313|Proteomes:UP000004512};
RX   PubMed=22408239; DOI=10.1128/JB.06664-11;
RA   Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT   "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL   J. Bacteriol. 194:1835-1836(2012).
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   -!- 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:EHK62382.1}.
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DR   EMBL; AHBC01000004; EHK62382.1; -; Genomic_DNA.
DR   RefSeq; WP_009095810.1; NZ_CP016490.1.
DR   AlphaFoldDB; H0IY91; -.
DR   STRING; 1118153.MOY_01649; -.
DR   MEROPS; M23.014; -.
DR   KEGG; hag:BB497_07590; -.
DR   PATRIC; fig|1118153.6.peg.327; -.
DR   eggNOG; COG0739; Bacteria.
DR   eggNOG; COG3061; Bacteria.
DR   OrthoDB; 9805070at2; -.
DR   Proteomes; UP000004512; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000004512};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          272..395
FT                   /note="Csd3-like second N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19425"
FT   DOMAIN          407..500
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   551 AA;  60592 MW;  B3610B2CFEDD49BE CRC64;
     MLRILHSLPR THKLLLLPVA TMVTVLGTQK LITTYNDLNQ PNTPLESVLV PLPSDSAPGV
     PSLRQERAPV AEAIGRASRA IDATRDHIPL SDLAATEIID LDIDLNVIAS AEASTTSESP
     MAKLDDGALH MAVVLGTLSS GMLNIDASSV EIADATSYED YGLFDDISFL EFELAAEEPF
     VPEWKTHIVE SGETFAVLAQ NKLGLGYSEV LALLEDLPDP RMLTHWRAGN SFDYQLDENQ
     RLLSLRMMKN ARDGVLLERE EEQYAVTTIE RQGEPVQRLY AGSVSGSFAR SAQATGLTSS
     SVTELTRLLE KKLDFRRDSR RGDRFQVLVE SDMIGGETLD SRVLAVKYDG ERMDLTVVRN
     ATDNNFYTPE GNSLDPAFAR YPFEGNYRLS SHFNPRRLHP VTGRVSPHNG TDFAMPIGTP
     IIAPANGRVE RVGNHHAAGR YIVVRHDNGY RTRYLHLSRP LVSQGERVEM GERIALSGNT
     GRSTGPHLHY EVIVNNTPVN AMTVDLPENT SLSGDTLIAF QRHAEPVLAA LESGETGPVN
     VAGYQREESS Q
//
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