ID Q2SHP3_HAHCH Unreviewed; 631 AA.
AC Q2SHP3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=Membrane protein related to metalloendopeptidase {ECO:0000313|EMBL:ABC29831.1};
GN OrderedLocusNames=HCH_03065 {ECO:0000313|EMBL:ABC29831.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC29831.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC29831.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC29831.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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DR EMBL; CP000155; ABC29831.1; -; Genomic_DNA.
DR RefSeq; WP_011396900.1; NC_007645.1.
DR AlphaFoldDB; Q2SHP3; -.
DR STRING; 349521.HCH_03065; -.
DR MEROPS; M23.001; -.
DR KEGG; hch:HCH_03065; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_446732_0_0_6; -.
DR OrthoDB; 6188067at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR000841; Pept_M23A_Blytic.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01551; Peptidase_M23; 1.
DR Pfam; PF04151; PPC; 2.
DR PRINTS; PR00933; BLYTICPTASE.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR600841-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..631
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004215448"
FT DOMAIN 263..330
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT DOMAIN 422..489
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT DOMAIN 533..599
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 374..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 264..310
FT /evidence="ECO:0000256|PIRSR:PIRSR600841-3"
FT DISULFID 354..367
FT /evidence="ECO:0000256|PIRSR:PIRSR600841-3"
SQ SEQUENCE 631 AA; 70180 MW; 3B1EF285547576C7 CRC64;
MKRMIKSILT CALTALPFFA QAYDSNAIPD DQFIYSYDEM LNFDVAAYLE EHAPHLKDQA
DVITHWAGYS SVSPKVLITL IEMQSGLLSR GERQFAAMQQ PMGDLSSESG FNAQVQDIAT
RLATNYYRTV GQEQQNLAFV GQGIATESLS DELRNNSEGD IEEFQEVYHR LFPETAQSTT
PSAAPALNRF AAYTRNALPP DNLLQLPFPV GEQWYFGGAH TYTGSGSYPL SSLDLNNGGY
WGSNTSNKWA AASAGGTAIR HSSCFVEVLH EGGWSTTYYH LDNIQFQNRA TVSRNQKLAN
YANNQSQALC DGGSSTGPHQ HFSLKYNGSY FHLEGVSLSG YKVKTGRWSY DGDCNYFWLS
KDNYRYCANR SLSNPGVPNG GDPTDGGDDN GGDDGGDDNS SETTLRNGQT VQNMSANKED
LTYYVLDVPA GSRNLYFKIS GGRGDVDMYV KRDGRPGFNN YNCRPYTTTQ DELCYYRTPQ
AGKYYIMLHA FSNYSGISLQ VGYENDNDQG NNREMSNGQV YRNLSGAQGE KSYFRLNVPA
GATDLRIEMS GGTGDADMHV MHQSQPTLSN YHCRPYSTKQ MEWCSWRYPY AGTFHIMLHA
FKPYSGIQLV ATYKTGSGAR ASMNLTEHME E
//
