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Database: UniProt
Entry: F7RMJ6_9GAMM
LinkDB: F7RMJ6_9GAMM
Original site: F7RMJ6_9GAMM 
ID   F7RMJ6_9GAMM            Unreviewed;       431 AA.
AC   F7RMJ6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Cell wall endopeptidase, family M23/M37 {ECO:0000313|EMBL:EGM70379.1};
GN   ORFNames=SOHN41_01587 {ECO:0000313|EMBL:EGM70379.1};
OS   Shewanella sp. HN-41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM70379.1, ECO:0000313|Proteomes:UP000002956};
RN   [1] {ECO:0000313|EMBL:EGM70379.1, ECO:0000313|Proteomes:UP000002956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HN-41 {ECO:0000313|EMBL:EGM70379.1,
RC   ECO:0000313|Proteomes:UP000002956};
RX   PubMed=21868804; DOI=10.1128/JB.05578-11;
RA   Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA   Hur H.G.;
RT   "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT   Arsenic-Sulfide Nanotubes.";
RL   J. Bacteriol. 193:5039-5040(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   -!- 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:EGM70379.1}.
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DR   EMBL; AFOZ01000019; EGM70379.1; -; Genomic_DNA.
DR   RefSeq; WP_007647274.1; NZ_AFOZ01000019.1.
DR   AlphaFoldDB; F7RMJ6; -.
DR   STRING; 327275.SOHN41_01587; -.
DR   MEROPS; M23.014; -.
DR   OrthoDB; 9805070at2; -.
DR   Proteomes; UP000002956; 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; 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          86..163
FT                   /note="Opacity-associated protein A"
FT                   /evidence="ECO:0000259|Pfam:PF04225"
FT   DOMAIN          169..292
FT                   /note="Csd3-like second N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19425"
FT   DOMAIN          304..398
FT                   /note="Peptidase M23"
FT                   /evidence="ECO:0000259|Pfam:PF01551"
SQ   SEQUENCE   431 AA;  47630 MW;  BC331F3412661173 CRC64;
     MQTGKPNFIN FSQTRLQNLS PAHKNILLVG GLLIGAAMLM PNANHVVPTA QRIPVVLDLD
     NILPQVSAPL EQESIIDNTP NFERIIASGD TLSSLFSKAG VDQQTMYKVL EADLNVLALD
     TLLPGNRMQF WLDNEGQLQK LELYFNAARQ VVFTRYEDGS FNVEEVNVEG VWQNRIVTGD
     IKGSFYVSAQ KMGLAAADIQ RIEDLLKEKV NFARDLRVGD KFSVLVNDQY VEGEATGSSQ
     ILGVSIKTGR SEISAFQHTD GSYYDAKGQS LVRAFQRIPL AKQPRMSSRF NPYRKHPITG
     RVSPHNGADF SVPIGTKIIA PGDGVVSLVT DHQFAGKYIV IEHGGKYRTR YLHLSKALVR
     KGQRVTRGQV IALSGNTGRS TGPHLHYEFH VNGKPVDPMK ADIPMASQLA NQELYNFANT
     VKSRQALMNL G
//
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