ID   MMPA_CAUVC              Reviewed;         398 AA.
AC   Q9A710;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Metalloprotease MmpA;
DE            EC=3.4.24.-;
DE   AltName: Full=Membrane metalloprotease A;
GN   Name=mmpA; OrderedLocusNames=CC_1916;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=15686556; DOI=10.1111/j.1365-2958.2004.04443.x;
RA   Chen J.C., Viollier P.H., Shapiro L.;
RT   "A membrane metalloprotease participates in the sequential degradation of a
RT   Caulobacter polarity determinant.";
RL   Mol. Microbiol. 55:1085-1103(2005).
CC   -!- FUNCTION: Involved in the regulated intramembrane proteolysis (RIP) of
CC       the short isoform of PodJ protein (PodJS), during the swarmer-to-
CC       stalked transition. The cleavage occurs near or within the single
CC       transmembrane of PodJS thereby releasing the N-terminal segment into
CC       the cytoplasm for subsequent degradation. It contributes to preserve
CC       asymmetry in the next cell cycle through sequential degradation.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle.
CC   -!- MISCELLANEOUS: Degradation of PodJS is not regulated by cyclic
CC       variation of MmpA level.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AE005673; AAK23891.1; -; Genomic_DNA.
DR   PIR; G87486; G87486.
DR   RefSeq; NP_420723.1; NC_002696.2.
DR   RefSeq; WP_010919782.1; NC_002696.2.
DR   AlphaFoldDB; Q9A710; -.
DR   SMR; Q9A710; -.
DR   STRING; 190650.CC_1916; -.
DR   EnsemblBacteria; AAK23891; AAK23891; CC_1916.
DR   KEGG; ccr:CC_1916; -.
DR   PATRIC; fig|190650.5.peg.1933; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_5; -.
DR   OMA; QYMVGFG; -.
DR   BioCyc; CAULO:CC1916-MON; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Differentiation; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..398
FT                   /note="Metalloprotease MmpA"
FT                   /id="PRO_0000088424"
FT   TRANSMEM        117..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          130..203
FT                   /note="PDZ"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000305"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   398 AA;  43231 MW;  D93795FD3AA1D6FA CRC64;
     MIGFLIMLVS LLFVLSVVVT VHELGHYWAA RACGVAIERF SIGFGAPLIS WRDKRGVEWC
     VASIPLGGYV RFAGDENAAS VPDQNDLDAM RNEIRRREGD DAVNRYFHFK PVWQRAFIAV
     AGPMANFILA ILVFAVILVS FGAQKTSTTV GEVVAGTPAA AAGFKPGDVI LKADNRQIRS
     FQDIQGYVAL RANMPIDFAV ERDGRTVHLT ATPRLVERQN EISGRVKVGE LGLRSAPGGR
     FERSSLLSAI PDATVEVWDM IKTIAFYLGR LLMGQLPADQ ISGIIGIGHT AGAVTNGVVE
     QAPNGKALAI GLIYSQFWLI ASLSVSIGFM NLLPIPVLDG GHLVMYAYEA VAKRPLRAEF
     QAAGFRAGLA LILGFMLFAA WNDLNRYDVF KFIGGLFT